Regulation of myosin light-chain phosphorylation and its roles in cardiovascular physiology and pathophysiology.
Myosin light chain kinase
Myosin light chain phosphorylation
Myosin phosphatase
Rho-kinase
RhoA
Journal
Hypertension research : official journal of the Japanese Society of Hypertension
ISSN: 1348-4214
Titre abrégé: Hypertens Res
Pays: England
ID NLM: 9307690
Informations de publication
Date de publication:
01 2022
01 2022
Historique:
received:
25
03
2021
accepted:
08
07
2021
revised:
19
06
2021
pubmed:
8
10
2021
medline:
28
1
2022
entrez:
7
10
2021
Statut:
ppublish
Résumé
The regulation of muscle contraction is a critical function in the cardiovascular system, and abnormalities may be life-threatening or cause illness. The common basic mechanism in muscle contraction is the interaction between the protein filaments myosin and actin. Although this interaction is primarily regulated by intracellular Ca
Identifiants
pubmed: 34616031
doi: 10.1038/s41440-021-00733-y
pii: 10.1038/s41440-021-00733-y
doi:
Substances chimiques
Myosin Light Chains
0
Myosin-Light-Chain Phosphatase
EC 3.1.3.53
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
40-52Informations de copyright
© 2021. The Author(s), under exclusive licence to The Japanese Society of Hypertension.
Références
Touyz RM, Alves-Lopes R, Rios FJ, Camargo LL, Anagnostopoulou A, Arner A, et al. Vascular smooth muscle contraction in hypertension. Cardiovasc Res. 2018;114:529–39.
pubmed: 29394331
pmcid: 5852517
doi: 10.1093/cvr/cvy023
Horowitz A, Menice CB, Laporte R, Morgan KG. Mechanisms of smooth muscle contraction. Physiol Rev. 1996;764:967–1003.
doi: 10.1152/physrev.1996.76.4.967
Somlyo AP, Somlyo AV. Signal transduction and regulation in smooth muscle. Nature. 1994;372:231–6.
pubmed: 7969467
doi: 10.1038/372231a0
Sweeney HL, Hammers DW. Muscle contraction. Cold Spring Harb Perspect Biol. 2018;102:a023200.
doi: 10.1101/cshperspect.a023200
Somlyo AP, Somlyo AV. Ca
doi: 10.1152/physrev.00023.2003
Kamm KE, Stull JT. Signaling to myosin regulatory light chain in sarcomeres. J Biol Chem. 2011;286:9941–7.
pubmed: 21257758
pmcid: 3060548
doi: 10.1074/jbc.R110.198697
Scruggs SB, Solaro RJ. The significance of regulatory light chain phosphorylation in cardiac physiology. Arch Biochem Biophys. 2011;510:129–34.
pubmed: 21345328
pmcid: 3114105
doi: 10.1016/j.abb.2011.02.013
Sheikh F, Lyon RC, Chen J. Getting the skinny on thick filament regulation in cardiac muscle biology and disease. Trends Cardiovasc Med. 2014;24:133–41.
pubmed: 23968570
doi: 10.1016/j.tcm.2013.07.004
Chang AN, Kamm KE, Stull JT. Role of myosin light chain phosphatase in cardiac physiology and pathophysiology. J Mol Cell Cardiol. 2016;101:35–43.
pubmed: 27742556
pmcid: 5154923
doi: 10.1016/j.yjmcc.2016.10.004
Liu Z, Khalil RA. Evolving mechanisms of vascular smooth muscle contraction highlight key targets in vascular disease. Biochem Pharm. 2018;153:91–122.
pubmed: 29452094
doi: 10.1016/j.bcp.2018.02.012
Herring BP, El-Mounayri O, Gallagher PJ, Yin F, Zhou J. Regulation of myosin light chain kinase and telokin expression in smooth muscle tissues. Am J Physiol Cell Physiol. 2006;291:C817–27.
pubmed: 16774989
doi: 10.1152/ajpcell.00198.2006
Ito M, Guerriero V Jr, Chen XM, Hartshorne DJ. Definition of the inhibitory domain of smooth muscle myosin light chain kinase by site-directed mutagenesis. Biochemistry. 1991;30:3498–503.
pubmed: 2012809
doi: 10.1021/bi00228a021
Hong F, Haldeman BD, Jackson D, Carter M, Baker JE, Cremo CR. Biochemistry of smooth muscle myosin light chain kinase. Arch Biochem Biophys. 2011;510:135–46.
pubmed: 21565153
pmcid: 3382066
doi: 10.1016/j.abb.2011.04.018
Kitazawa T, Gaylinn BD, Denney GH, Somlyo AP. G-protein-mediated Ca
doi: 10.1016/S0021-9258(18)52353-X
Bradley AB, Morgan KG. Alterations in cytoplasmic calcium sensitivity during porcine coronary artery contractions as detected by aequorin. J Physiol. 1987;385:437–48.
pubmed: 3477639
pmcid: 1192353
doi: 10.1113/jphysiol.1987.sp016500
Shimokawa H, Sunamura S, Satoh K. RhoA/Rho-kinase in the cardiovascular system. Circ Res. 2016;118:352–66.
pubmed: 26838319
doi: 10.1161/CIRCRESAHA.115.306532
Loirand G, Guérin P, Pacaud P. Rho kinases in cardiovascular physiology and pathophysiology. Circ Res. 2006;98:322–34.
pubmed: 16484628
doi: 10.1161/01.RES.0000201960.04223.3c
Alessi D, MacDougall LK, Sola MM, Ikebe M, Cohen P. The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1. Eur J Biochem. 1992;210:1023–35.
pubmed: 1336455
doi: 10.1111/j.1432-1033.1992.tb17508.x
Shimizu H, Ito M, Miyahara M, Ichikawa K, Okubo S, Konishi T, et al. Characterization of the myosin-binding subunit of smooth muscle myosin phosphatase. J Biol Chem. 1994;269:30407–11.
pubmed: 7982954
doi: 10.1016/S0021-9258(18)43828-8
Takahashi N, Ito M, Tanaka J, Nakano T, Kaibuchi K, Odai H, et al. Localization of the gene coding for myosin phosphatase, target subunit 1 (MYPT1) to human chromosome 12q15-q21. Genomics. 1997;44:150–2.
pubmed: 9286714
doi: 10.1006/geno.1997.4859
Chen YH, Chen MX, Alessi DR, Campbell DG, Shanahan C, Cohen P, et al. Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory subunits of smooth muscle protein phosphatase 1 M. FEBS Lett. 1994;356:51–5.
pubmed: 7988720
doi: 10.1016/0014-5793(94)01231-8
Hartshorne DJ, Ito M, Erdödi F. Myosin light chain phosphatase: subunit composition, interactions and regulation. J Muscle Res Cell Motil. 1998;19:325–41.
pubmed: 9635276
doi: 10.1023/A:1005385302064
Hartshorne DJ, Ito M, Erdödi F. Role of protein phosphatase type 1 in contractile functions: Myosin phosphatase. J Biol Chem. 2004;279:37211–4.
pubmed: 15136561
doi: 10.1074/jbc.R400018200
Ito M, Nakano T, Erdodi F, Hartshorne DJ. Myosin phosphatase: structure, regulation and function. Mol Cell Biochem. 2004;259:197–209.
pubmed: 15124925
doi: 10.1023/B:MCBI.0000021373.14288.00
Grassie ME, Moffat LD, Walsh MP, MacDonald JA. The myosin phosphatase targeting protein (MYPT) family: a regulated mechanism for achieving substrate specificity of the catalytic subunit of protein phosphatase type 1δ. Arch Biochem Biophys. 2011;510:147–59.
pubmed: 21291858
doi: 10.1016/j.abb.2011.01.018
Kiss A, Erdődi F, Lontay B. Myosin phosphatase: unexpected functions of a long-known enzyme. Biochim Biophys Acta Mol Cell Res. 2019;1866:2–15.
pubmed: 30076859
doi: 10.1016/j.bbamcr.2018.07.023
Tanaka J, Ito M, Feng J, Ichikawa K, Hamaguchi T, Nakamura M, et al. Interaction of myosin phosphatase target subunit 1 with the catalytic subunit of type 1 protein phosphatase. Biochemistry. 1998;37:16697–703.
pubmed: 9843438
doi: 10.1021/bi980782x
Ichikawa K, Hirano K, Ito M, Tanaka J, Nakano T, Hartshorne DJ. Interactions and properties of smooth muscle myosin phosphatase. Biochemistry. 1996;35:6313–20.
pubmed: 8639575
doi: 10.1021/bi960208q
Kimura K, Ito M, Amano M, Chihara K, Fukata Y, Nakafuku M, et al. Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase). Science. 1996;273:245–8.
pubmed: 8662509
doi: 10.1126/science.273.5272.245
Surks HK, Mochizuki N, Kasai Y, Georgescu SP, Tang KM, Ito M, et al. Regulation of myosin phosphatase by a specific interaction with cGMP-dependent protein kinase Iα. Science. 1999;286:1583–7.
pubmed: 10567269
doi: 10.1126/science.286.5444.1583
Ichikawa K, Ito M, Hartshorne DJ. Phosphorylation of the large subunit of myosin phosphatase and inhibition of phosphatase activity. J Biol Chem. 1996;27:4733–40.
doi: 10.1074/jbc.271.9.4733
Matsui T, Amano M, Yamamoto T, Chihara K, Nakafuku M, Ito M, et al. Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho. EMBO J. 1996;15:2208–16.
pubmed: 8641286
pmcid: 450144
doi: 10.1002/j.1460-2075.1996.tb00574.x
Eto M, Ohmori T, Suzuki M, Furuya K, Morita F. A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization. J Biochem. 1995;118:1104–7.
pubmed: 8720121
doi: 10.1093/oxfordjournals.jbchem.a124993
Eto M, Senba S, Morita F, Yazawa M. Molecular cloning of a novel phosphorylation-dependent inhibitory protein of protein phosphatase-1 (CPI17) in smooth muscle: Its specific localization in smooth muscle. FEBS Lett. 1997;410:356–60.
pubmed: 9237662
doi: 10.1016/S0014-5793(97)00657-1
Leung T, Manser E, Tan L, Lim L. A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes. J Biol Chem. 1995;270:29051–4.
pubmed: 7493923
doi: 10.1074/jbc.270.49.29051
Ishizaki T, Maekawa M, Fujisawa K, Okawa K, Iwamatsu A, Fujita A, et al. The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase. EMBO J. 1996;15:1885–93.
pubmed: 8617235
pmcid: 450107
doi: 10.1002/j.1460-2075.1996.tb00539.x
Fukata Y, Amano M, Kaibuchi K. Rho-Rho-kinase pathway in smooth muscle contraction and cytoskeletal reorganization of non-muscle cells. Trends Pharm Sci. 2001;22:32–9.
pubmed: 11165670
doi: 10.1016/S0165-6147(00)01596-0
Amano M, Nakayama M, Kaibuchi K. Rho-kinase/ROCK: a key regulator of the cytoskeleton and cell polarity. Cytoskeleton. 2010;67:545–54.
pubmed: 20803696
doi: 10.1002/cm.20472
Feng J, Ito M, Ichikawa K, Isaka N, Nishikawa M, Hartshorne DJ, et al. Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase. J Biol Chem. 1999;274:37385–90.
pubmed: 10601309
doi: 10.1074/jbc.274.52.37385
Khromov A, Choudhury N, Stevenson AS, Somlyo AV, Eto M. Phosphorylation-dependent autoinhibition of myosin light chain phosphatase accounts for Ca
pubmed: 19531490
pmcid: 2755881
doi: 10.1074/jbc.M109.019729
Khasnis M, Nakatomi A, Gumpper K, Eto M. Reconstituted human myosin light chain phosphatase reveals distinct roles of two inhibitory phosphorylation sites of the regulatory subunit, MYPT1. Biochemistry. 2014;53:2701–9.
pubmed: 24712327
doi: 10.1021/bi5001728
Velasco G, Armstrong C, Morrice N, Frame S, Cohen P. Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1 M at Thr850 induces its dissociation from myosin. FEBS Lett. 2002;527:101–4.
pubmed: 12220642
doi: 10.1016/S0014-5793(02)03175-7
Murányi A, Derkach D, Erdodi F, Kiss A, Ito M, Hartshorne DJ. Phosphorylation of Thr695 and Thr850 on the myosin phosphatase target subunit: inhibitory effects and occurrence in A7r5 cells. FEBS Lett. 2005;579:6611–5.
pubmed: 16297917
doi: 10.1016/j.febslet.2005.10.055
Kiss E, Murányi A, Csortos C, Gergely P, Ito M, Hartshorne DJ, et al. Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton. Biochem J. 2002;365:79–87.
pubmed: 11931630
pmcid: 1222641
doi: 10.1042/bj20011295
Murányi A, Zhang R, Liu F, Hirano K, Ito M, Epstein HF, et al. Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activity. FEBS Lett. 2001;493:80–4.
pubmed: 11287000
doi: 10.1016/S0014-5793(01)02283-9
MacDonald JA, Borman MA, Murányi A, Somlyo AV, Hartshorne DJ, Haystead TA. Identification of the endogenous smooth muscle myosin phosphatase-associated kinase. Proc Natl Acad Sci USA. 2001;98:2419–24.
pubmed: 11226254
pmcid: 30153
doi: 10.1073/pnas.041331498
Butler T, Paul J, Europe-Finner N, Smith R, Chan EC. Role of serine-threonine phosphoprotein phosphatases in smooth muscle contractility. Am J Physiol Cell Physiol. 2013;304:C485–504.
pubmed: 23325405
doi: 10.1152/ajpcell.00161.2012
Niiro N, Koga Y, Ikebe M. Agonist-induced changes in the phosphorylation of the myosin- binding subunit of myosin light chain phosphatase and CPI17, two regulatory factors of myosin light chain phosphatase, in smooth muscle. Biochem J. 2003;369:117–28.
pubmed: 12296769
pmcid: 1223061
doi: 10.1042/bj20021040
Kitazawa T, Eto M, Woodsome TP, Khalequzzaman M. Phosphorylation of the myosin phosphatase targeting subunit and CPI-17 during Ca
pubmed: 12563012
doi: 10.1113/jphysiol.2002.029306
Wilson DP, Susnjar M, Kiss E, Sutherland C, Walsh MP. Thromboxane A
pubmed: 15823093
pmcid: 1180727
doi: 10.1042/BJ20050237
Tsai MH, Chang AN, Huang J, He W, Sweeney HL, Zhu M, et al. Constitutive phosphorylation of myosin phosphatase targeting subunit-1 in smooth muscle. J Physiol. 2014;592:3031–51.
pubmed: 24835173
pmcid: 4214658
doi: 10.1113/jphysiol.2014.273011
Chen CP, Chen X, Qiao YN, Wang P, He WQ, Zhang CH, et al. In vivo roles for myosin phosphatase targeting subunit-1 phosphorylation sites T694 and T852 in bladder smooth muscle contraction. J Physiol. 2015;593:681–700.
pubmed: 25433069
doi: 10.1113/jphysiol.2014.283853
Li L, Eto M, Lee MR, Morita F, Yazawa M, Kitazawa T. Possible involvement of the novel CPI-17 protein in protein kinase C signal transduction of rabbit arterial smooth muscle. J Physiol. 1998;508:871–81.
pubmed: 9518739
pmcid: 2230912
doi: 10.1111/j.1469-7793.1998.871bp.x
Eto M. Regulation of cellular protein phosphatase-1 (PP1) by phosphorylation of the CPI-17 family, C-kinase-activated PP1 inhibitors. J Biol Chem. 2009;284:35273–7.
pubmed: 19846560
pmcid: 2790955
doi: 10.1074/jbc.R109.059972
Eto M, Kitazawa T. Diversity and plasticity in signaling pathways that regulate smooth muscle responsiveness: paradigms and paradoxes for the myosin phosphatase, the master regulator of smooth muscle contraction. J Smooth Muscle Res. 2017;53:1–19.
pubmed: 28260704
pmcid: 5364378
doi: 10.1540/jsmr.53.1
Machida H, Ito M, Okamoto R, Shiraki K, Isaka N, Hartshorne DJ, et al. Molecular cloning and analysis of the 5’-flanking region of the human MYPT1 gene. Biochim Biophys Acta. 2001;1517:424–9.
pubmed: 11342221
doi: 10.1016/S0167-4781(00)00285-2
Koyama M, Ito M, Feng J, Seko T, Shiraki K, Takase K, et al. Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase. FEBS Lett. 2000;475:197–200.
pubmed: 10869555
doi: 10.1016/S0014-5793(00)01654-9
Hamaguchi T, Ito M, Feng J, Seko T, Koyama M, Machida H, et al. Phosphorylation of CPI-17, an inhibitor of myosin phosphatase, by protein kinase N. Biochem Biophys Res Commun. 2000;274:825–30.
pubmed: 10924361
doi: 10.1006/bbrc.2000.3225
Kitazawa T, Eto M, Woodsome TP, Brautigan DL. Agonists trigger G protein-mediated activation of the CPI-17 inhibitor phosphoprotein of myosin light chain phosphatase to enhance vascular smooth muscle contractility. J Biol Chem. 2000;275:9897–900.
pubmed: 10744661
doi: 10.1074/jbc.275.14.9897
Shin HM, Je HD, Gallant C, Tao TC, Hartshorne DJ, Ito M, et al. Differential association and localization of myosin phosphatase subunits during agonist-induced signal transduction in smooth muscle. Circ Res. 2002;90:546–53.
pubmed: 11909818
doi: 10.1161/01.RES.0000012822.23273.EC
Amano M, Ito M, Kimura K, Fukata Y, Chihara K, Nakano T, et al. Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase). J Biol Chem. 1996;271:20246–9.
pubmed: 8702756
doi: 10.1074/jbc.271.34.20246
Kureishi Y, Kobayashi S, Amano M, Kimura K, Kanaide H, Nakano T, et al. Rho-associated kinase directly induces smooth muscle contraction through myosin light chain phosphorylation. J Biol Chem. 1997;272:12257–60.
pubmed: 9139666
doi: 10.1074/jbc.272.19.12257
Deng JT, Bhaidani S, Sutherland C, MacDonald JA, Walsh MP. Rho-associated kinase and zipper-interacting protein kinase, but not myosin light chain kinase, are involved in the regulation of myosin phosphorylation in serum-stimulated human arterial smooth muscle cells. PLoS ONE. 2019;14:e0226406.
pubmed: 31834925
pmcid: 6910671
doi: 10.1371/journal.pone.0226406
Walsh MP. Vascular smooth muscle myosin light chain diphosphorylation: mechanism, function, and pathological implications. IUBMB Life. 2011;63:987–1000.
pubmed: 21990256
doi: 10.1002/iub.527
Carvajal JA, Germain AM, Huidobro-Toro JP, Weiner CP. Molecular mechanism of cGMP-mediated smooth muscle relaxation. J Cell Physiol. 2000;184:409–20.
pubmed: 10911373
doi: 10.1002/1097-4652(200009)184:3<409::AID-JCP16>3.0.CO;2-K
Morgado M, Cairrão E, Santos-Silva AJ, Verde I. Cyclic nucleotide-dependent relaxation pathways in vascular smooth muscle. Cell Mol Life Sci. 2012;69:247–66.
pubmed: 21947498
doi: 10.1007/s00018-011-0815-2
Lee MR, Li L, Kitazawa T. Cyclic GMP causes Ca
pubmed: 9030570
doi: 10.1074/jbc.272.8.5063
Khatri JJ, Joyce KM, Brozovich FV, Fisher SA. Role of myosin phosphatase isoforms in cGMP-mediated smooth muscle relaxation. J Biol Chem. 2001;276:37250–7.
pubmed: 11486008
doi: 10.1074/jbc.M105275200
Dippold RP, Fisher SA. Myosin phosphatase isoforms as determinants of smooth muscle contractile function and calcium sensitivity of force production. Microcirculation. 2014;21:239–48.
pubmed: 24112301
pmcid: 4349328
doi: 10.1111/micc.12097
Vetterkind S, Lee E, Sundberg E, Poythress RH, Tao TC, Preuss U, et al. Par-4: a new activator of myosin phosphatase. Mol Biol Cell. 2010;21:1214–24.
pubmed: 20130087
pmcid: 2847525
doi: 10.1091/mbc.e09-08-0711
Nakamura M, Ichikawa K, Ito M, Yamamori B, Okinaka T, Isaka N, et al. Effects of the phosphorylation of myosin phosphatase by cyclic GMP-dependent protein kinase. Cell Signal. 1999;11:671–6.
pubmed: 10530875
doi: 10.1016/S0898-6568(99)00036-4
Ito M, Feng J, Tsujino S, Inagaki N, Inagaki M, Tanaka J, et al. Interaction of smooth muscle myosin phosphatase with phospholipids. Biochemistry. 1997;36:7607–14.
pubmed: 9200713
doi: 10.1021/bi9702647
Wooldridge AA, MacDonald JA, Erdodi F, Ma C, Borman MA, Hartshorne DJ, et al. Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides. J Biol Chem. 2004;279:34496–504.
pubmed: 15194681
doi: 10.1074/jbc.M405957200
Grassie ME, Sutherland C, Ulke-Lemée A, Chappellaz M, Kiss E, Walsh MP, et al. Cross-talk between Rho-associated kinase and cyclic nucleotide-dependent kinase signaling pathways in the regulation of smooth muscle myosin light chain phosphatase. J Biol Chem. 2012;287:36356–69.
pubmed: 22948155
pmcid: 3476302
doi: 10.1074/jbc.M112.398479
Inagaki N, Nishizawa M, Ito M, Fujioka M, Nakano T, Tsujino S, et al. Myosin binding subunit of smooth muscle myosin phosphatase at the cell-cell adhesion sites in MDCK cells. Biochem Biophys Res Commun. 1997;230:552–6.
pubmed: 9015360
doi: 10.1006/bbrc.1996.5986
Qiao YN, He WQ, Chen CP, Zhang CH, Zhao W, Wang P, et al. Myosin phosphatase target subunit 1 (MYPT1) regulates the contraction and relaxation of vascular smooth muscle and maintains blood pressure. J Biol Chem. 2014;289:22512–23.
pubmed: 24951589
pmcid: 4139257
doi: 10.1074/jbc.M113.525444
Etter EF, Eto M, Wardle RL, Brautigan DL, Murphy RA. Activation of myosin light chain phosphatase in intact arterial smooth muscle during nitric oxide-induced relaxation. J Biol Chem. 2001;276:34681–5.
pubmed: 11461918
doi: 10.1074/jbc.M104737200
Kitazawa T, Semba S, Yang Huh YH, Kitazawa K, Eto M. Nitric oxide-induced biphasic mechanism of vascular relaxation via dephosphorylation of CPI-17 and MYPT1. J Physiol. 2009;587:3587–603.
pubmed: 19470783
pmcid: 2742283
doi: 10.1113/jphysiol.2009.172189
Sandu OA, Ito M, Begum N. Selected contribution: Insulin utilizes NO/cGMP pathway to activate myosin phosphatase via Rho inhibition in vascular smooth muscle. J Appl Physiol. 2001;91:1475–82.
pubmed: 11509551
doi: 10.1152/jappl.2001.91.3.1475
Begum N, Sandu OA, Ito M, Lohmann SM, Smolenski A. Active Rho kinase (ROK-α) associates with insulin receptor substrate-1 and inhibits insulin signaling in vascular smooth muscle cells. J Biol Chem. 2002;277:6214–22.
pubmed: 11739394
doi: 10.1074/jbc.M110508200
Ito M, Dabrowska R, Guerriero V Jr, Hartshorne DJ. Identification in turkey gizzard of an acidic protein related to the C-terminal portion of smooth muscle myosin light chain kinase. J Biol Chem. 1989;264:13971–4.
pubmed: 2760053
doi: 10.1016/S0021-9258(18)71627-X
Khromov AS, Wang H, Choudhury N, McDuffie M, Herring BP, Nakamoto R, et al. Smooth muscle of telokin-deficient mice exhibits increased sensitivity to Ca
pubmed: 16461919
pmcid: 1413704
doi: 10.1073/pnas.0508566103
Khromov AS, Momotani K, Jin L, Artamonov MV, Shannon J, Eto M, et al. Molecular mechanism of telokin-mediated disinhibition of myosin light chain phosphatase and cAMP/cGMP-induced relaxation of gastrointestinal smooth muscle. J Biol Chem. 2012;287:20975–85.
pubmed: 22544752
pmcid: 3375521
doi: 10.1074/jbc.M112.341479
Nobe K, Paul RJ. Distinct pathways of Ca
pubmed: 11420305
doi: 10.1161/hh1201.092035
Dimopoulos GJ, Semba S, Kitazawa K, Eto M, Kitazawa T. Ca
pubmed: 17158339
doi: 10.1161/01.RES.0000253902.90489.df
Raina H, Zacharia J, Li M, Wier WG. Activation by Ca
pubmed: 19403597
pmcid: 2714024
doi: 10.1113/jphysiol.2008.165258
Kitazawa T, Kitazawa K. Size-dependent heterogeneity of contractile Ca
pubmed: 22930267
pmcid: 3515827
doi: 10.1113/jphysiol.2012.241315
Davis MJ, Hill MA. Signaling mechanisms underlying the vascular myogenic response. Physiol Rev. 1999;79:387–423.
pubmed: 10221985
doi: 10.1152/physrev.1999.79.2.387
Hill MA, Zou H, Potocnik SJ, Meininger GA, Davis MJ. Invited review: arteriolar smooth muscle mechanotransduction: Ca
pubmed: 11457816
doi: 10.1152/jappl.2001.91.2.973
Schubert R, Lidington D, Bolz SS. The emerging role of Ca
pubmed: 17764667
Cole WC, Welsh DG. Role of myosin light chain kinase and myosin light chain phosphatase in the resistance arterial myogenic response to intravascular pressure. Arch Biochem Biophys. 2011;510:160–73.
pubmed: 21392499
doi: 10.1016/j.abb.2011.02.024
Zou H, Ratz PH, Hill MA. Role of myosin phosphorylation and [Ca
pubmed: 7503253
Hill MA, Falcone JC, Meininger GA. Evidence for protein kinase C involvement in arteriolar myogenic reactivity. Am J Physiol. 1990;259:H1586–H1594.
pubmed: 2240255
Karibe A, Watanabe J, Horiguchi S, Takeuchi M, Suzuki S, Funakoshi M, et al. Role of cytosolic Ca
pubmed: 9087589
Wesselman JP, Spaan JA, van der Meulen ET, VanBavel E. Role of protein kinase C in myogenic calcium-contraction coupling of rat cannulated mesenteric small arteries. Clin Exp Pharm Physiol. 2001;28:848–55.
doi: 10.1046/j.1440-1681.2001.03534.x
Lagaud G, Gaudreault N, Moore ED, Van Breemen C, Laher I. Pressure-dependent myogenic constriction of cerebral arteries occurs independently of voltage-dependent activation. Am J Physiol Heart Circ Physiol. 2002;283:H2187–H2195.
pubmed: 12388215
doi: 10.1152/ajpheart.00554.2002
Bolz SS, Vogel L, Sollinger D, Derwand R, Boer C, Pitson SM, et al. Sphingosine kinase modulates microvascular tone and myogenic responses through activation of RhoA/Rho kinase. Circulation. 2003;108:342–7.
pubmed: 12847068
doi: 10.1161/01.CIR.0000080324.12530.0D
Dubroca C, Loyer X, Retailleau K, Loirand G, Pacaud P, Feron O, et al. RhoA activation and interaction with caveolin-1 are critical for pressure-induced myogenic tone in rat mesenteric resistance arteries. Cardiovasc Res. 2007;73:190–7.
pubmed: 17150200
doi: 10.1016/j.cardiores.2006.10.020
El-Yazbi AF, Abd-Elrahman KS. ROK and arteriolar myogenic tone generation: molecular evidence in health and disease. Front Pharm. 2017;8:87.
doi: 10.3389/fphar.2017.00087
Johnson RP, El-Yazbi AF, Takeya K, Walsh EJ, Walsh MP, Cole WC. Ca
pubmed: 19359365
pmcid: 2714019
doi: 10.1113/jphysiol.2008.168252
El-Yazbi AF, Johnson RP, Walsh EJ, Takeya K, Walsh MP, Cole WC. Pressure-dependent contribution of Rho kinase-mediated calcium sensitization in serotonin-evoked vasoconstriction of rat cerebral arteries. J Physiol. 2010;588:1747–62.
pubmed: 20351047
pmcid: 2887992
doi: 10.1113/jphysiol.2010.187146
Moreno-Domínguez A, Colinas O, El-Yazbi A, Walsh EJ, Hill MA, Walsh MP, et al. Ca
pubmed: 23230233
doi: 10.1113/jphysiol.2012.243576
Lee DL, Webb RC, Jin L. Hypertension and RhoA/Rho-kinase signaling in the vasculature: highlights from the recent literature. Hypertension. 2004;44:796–9.
pubmed: 15520302
doi: 10.1161/01.HYP.0000148303.98066.ab
Han YJ, Hu WY, Chernaya O, Antic N, Gu L, Gupta M, et al. Increased myosin light chain kinase expression in hypertension: Regulation by serum response factor via an insertion mutation in the promoter. Mol Biol Cell. 2006;17:4039–50.
pubmed: 16822834
pmcid: 1593173
doi: 10.1091/mbc.e06-04-0353
Hu WY, Han YJ, Gu L, Piano M, de Lanerolle P. Involvement of Ras-regulated myosin light chain phosphorylation in the captopril effects in spontaneously hypertensive rats. Am J Hypertens. 2007;20:53–61.
pubmed: 17198912
doi: 10.1016/j.amjhyper.2006.05.024
He WQ, Peng YJ, Zhang WC, Lv N, Tang J, Chen C, et al. Myosin light chain kinase is central to smooth muscle contraction and required for gastrointestinal motility in mice. Gastroenterology. 2008;1352:610–20.
doi: 10.1053/j.gastro.2008.05.032
He WQ, Qiao YN, Zhang CH, Peng YJ, Chen C, Wang P, et al. Role of myosin light chain kinase in regulation of basal blood pressure and maintenance of salt-induced hypertension. Am J Physiol Heart Circ Physiol. 2011;3012:H584–H591.
doi: 10.1152/ajpheart.01212.2010
Wang L, Guo DC, Cao J, Gong L, Kamm KE, Regalado E, et al. Mutations in myosin light chain kinase cause familial aortic dissections. Am J Hum Genet. 2010;87:701–7.
pubmed: 21055718
pmcid: 2978973
doi: 10.1016/j.ajhg.2010.10.006
Okamoto R, Ito M, Suzuki N, Kongo M, Moriki N, Saito H, et al. The targeted disruption of the MYPT1 gene results in embryonic lethality. Transgenic Res. 2005;14:337–40.
pubmed: 16145842
doi: 10.1007/s11248-005-3453-3
He WQ, Qiao YN, Peng YJ, Zha JM, Zhang CH, Chen C, et al. Altered contractile phenotypes of intestinal smooth muscle in mice deficient in myosin phosphatase target subunit 1. Gastroenterology. 2013;144:1456–65.
pubmed: 23499953
doi: 10.1053/j.gastro.2013.02.045
Hughes JJ, Alkhunaizi E, Kruszka P, Pyle LC, Grange DK, Berger SI, et al. Loss-of-function variants in PPP1R12A: from isolated sex reversal to holoprosencephaly spectrum and urogenital malformations. Am J Hum Genet. 2020;106:121–8.
pubmed: 31883643
doi: 10.1016/j.ajhg.2019.12.004
Uehata M, Ishizaki T, Satoh H, Ono T, Kawahara T, Morishita T, et al. Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension. Nature. 1997;389:990–4.
pubmed: 9353125
doi: 10.1038/40187
Seko T, Ito M, Kureishi Y, Okamoto R, Moriki N, Onishi K, et al. Activation of RhoA and inhibition of myosin phosphatase as important components in hypertension in vascular smooth muscle. Circ Res. 2003;92:411–8.
pubmed: 12600888
doi: 10.1161/01.RES.0000059987.90200.44
Chrissobolis S, Sobey CG. Evidence that Rho-kinase activity contributes to cerebral vascular tone in vivo and is enhanced during chronic hypertension: Comparison with protein kinase C. Circ Res. 2001;88:774–9.
pubmed: 11325868
doi: 10.1161/hh0801.090441
Moriki N, Ito M, Seko T, Kureishi Y, Okamoto R, Nakakuki T, et al. RhoA activation in vascular smooth muscle cells from stroke-prone spontaneously hypertensive rats. Hypertens Res. 2004;27:263–70.
pubmed: 15127884
doi: 10.1291/hypres.27.263
Crestani S, Webb RC, da Silva-Santos JE. High-salt intake augments the activity of the RhoA/ROCK pathway and reduces intracellular calcium in arteries from rats. Am J Hypertens. 2017;30:389–99.
pubmed: 28164209
pmcid: 5861573
doi: 10.1093/ajh/hpw201
Booden MA, Siderovski DP, Der CJ. Leukemia-associated Rho guanine nucleotide exchange factor promotes Gαq-coupled activation of RhoA. Mol Cell Biol. 2002;22:4053–61.
pubmed: 12024019
pmcid: 133844
doi: 10.1128/MCB.22.12.4053-4061.2002
Sakurada S, Takuwa N, Sugimoto N, Wang Y, Seto M, Sasaki Y, et al. Ca
pubmed: 12919947
doi: 10.1161/01.RES.0000090998.08629.60
Siehler S. Regulation of RhoGEF proteins by G
doi: 10.1111/j.1476-5381.2009.00121.x
Cherfils J, Zeghouf M. Regulation of small GTPases by GEFs, GAPs, and GDIs. Physiol Rev. 2013;93:269–309.
pubmed: 23303910
doi: 10.1152/physrev.00003.2012
Wirth A, Benyó Z, Lukasova M, Leutgeb B, Wettschureck N, Gorbey S, et al. G
pubmed: 18084302
doi: 10.1038/nm1666
Guilluy C, Brégeon J, Toumaniantz G, Rolli-Derkinderen M, Retailleau K, Loufrani L, et al. The Rho exchange factor Arhgef1 mediates the effects of angiotensin II on vascular tone and blood pressure. Nat Med. 2010;16:183–90.
pubmed: 20098430
doi: 10.1038/nm.2079
Ying Z, Jin L, Dorrance AM, Webb RC. Increased expression of mRNA for regulator of G protein signaling domain-containing Rho guanine nucleotide exchange factors in aorta from stroke-prone spontaneously hypertensive rats. Am J Hypertens. 2004;17:981–5.
pubmed: 15485764
doi: 10.1016/j.amjhyper.2004.05.006
Bai X, Lenhart KC, Bird KE, Suen AA, Rojas M, Kakoki M, et al. The smooth muscle-selective RhoGAP GRAF3 is a critical regulator of vascular tone and hypertension. Nat Commun. 2013;4:2910.
pubmed: 24335996
doi: 10.1038/ncomms3910
Masumoto A, Hirooka Y, Shimokawa H, Hironaga K, Setoguchi S, Takeshita A. Possible involvement of Rho-kinase in the pathogenesis of hypertension in humans. Hypertension. 2001;38:1307–10.
pubmed: 11751708
doi: 10.1161/hy1201.096541
Momotani K, Somlyo AV. 63RhoGEF: a new switch for G
pubmed: 22902181
pmcid: 3472095
doi: 10.1016/j.tcm.2012.07.007
Calò LA, Davis PA, Pagnin E, Dal ML, Maiolino G, Seccia TM, et al. Increased level of p63RhoGEF and RhoA/Rho kinase activity in hypertensive patients. J Hypertens. 2014;32:331–8.
pubmed: 24356540
doi: 10.1097/HJH.0000000000000075
Carbone ML, Brégeon J, Devos N, Chadeuf G, Blanchard A, Azizi M, et al. Angiotensin II activates the RhoA exchange factor Arhgef1 in humans. Hypertension. 2015;65:1273–8.
pubmed: 25870189
doi: 10.1161/HYPERTENSIONAHA.114.05065
Su W, Xie Z, Liu S, Calderon LE, Guo Z, Gong MC. Smooth muscle-selective CPI-17 expression increases vascular smooth muscle contraction and blood pressure. Am J Physiol Heart Circ Physiol. 2013;305:H104–13.
pubmed: 23604714
pmcid: 3727105
doi: 10.1152/ajpheart.00597.2012
Yang Q, Fujii W, Kaji N, Kakuta S, Kada K, Kuwahara M, et al. The essential role of phospho-T38 CPI-17 in the maintenance of physiological blood pressure using genetically modified mice. FASEB J. 2018;32:2095–109.
pubmed: 29229685
doi: 10.1096/fj.201700794R
Sun J, Tao T, Zhao W, Wei L, She F, Wang P, et al. CPI-17-mediated contraction of vascular smooth muscle is essential for the development of hypertension in obese mice. J Genet Genomics. 2019;46:109–18.
pubmed: 30948334
doi: 10.1016/j.jgg.2019.02.005
Xie Z, Su W, Guo Z, Pang H, Post SR, Gong MC. Up-regulation of CPI-17 phosphorylation in diabetic vasculature and high glucose cultured vascular smooth muscle cells. Cardiovasc Res. 2006;69:491–501.
pubmed: 16336954
doi: 10.1016/j.cardiores.2005.11.002
Kizub IV, Pavlova OO, Johnson CD, Soloviev AI, Zholos AV. Rho kinase and protein kinase C involvement in vascular smooth muscle myofilament calcium sensitization in arteries from diabetic rats. Br J Pharm. 2010;159:1724–31.
doi: 10.1111/j.1476-5381.2010.00666.x
Lubomirov LT, Gagov H, Schroeter MM, Wiesner RJ, Franko A. Augmented contractility of murine femoral arteries in a streptozotocin diabetes model is related to increased phosphorylation of MYPT1. Physiol Rep. 2019;7:e13975.
pubmed: 30740930
pmcid: 6369311
doi: 10.14814/phy2.13975
Fukumoto Y, Matoba T, Ito A, Tanaka H, Kishi T, Hayashidani S, et al. Acute vasodilator effects of a Rho-kinase inhibitor, fasudil, in patients with severe pulmonary hypertension. Heart. 2005;91:391–2.
pubmed: 15710736
pmcid: 1768747
doi: 10.1136/hrt.2003.029470
Ishikura K, Yamada N, Ito M, Ota S, Nakamura M, Isaka N, et al. Beneficial acute effects of rho-kinase inhibitor in patients with pulmonary arterial hypertension. Circ J. 2006;70:174–8.
pubmed: 16434811
doi: 10.1253/circj.70.174
Oka M, Homma N, Taraseviciene-Stewart L, Morris KG, Kraskauskas D, Burns N, et al. Rho kinase-mediated vasoconstriction is important in severe occlusive pulmonary arterial hypertension in rats. Circ Res. 2007;100:923–9.
pubmed: 17332430
doi: 10.1161/01.RES.0000261658.12024.18
Oka M, Fagan KA, Jones PL, McMurtry IF. Therapeutic potential of RhoA/Rho kinase inhibitors in pulmonary hypertension. Br J Pharm. 2008;155:444–54.
doi: 10.1038/bjp.2008.239
Barman SA, Zhu S, White RE. RhoA/Rho-kinase signaling: a therapeutic target in pulmonary hypertension. Vasc Health Risk Manag. 2009;5:663–71.
pubmed: 19707285
pmcid: 2731064
doi: 10.2147/VHRM.S4711
Guilluy C, Sauzeau V, Rolli-Derkinderen M, Guérin P, Sagan C, Pacaud P, et al. Inhibition of RhoA/Rho kinase pathway is involved in the beneficial effect of sildenafil on pulmonary hypertension. Br J Pharm. 2005;146:1010–8.
doi: 10.1038/sj.bjp.0706408
Do e Z, Fukumoto Y, Takaki A, Tawara S, Ohashi J, Nakano M, et al. Evidence for Rho-kinase activation in patients with pulmonary arterial hypertension. Circ J. 2009;73:1731–9.
doi: 10.1253/circj.CJ-09-0135
Shimizu T, Fukumoto Y, Tanaka S, Satoh K, Ikeda S, Shimokawa H. Crucial role of ROCK2 in vascular smooth muscle cells for hypoxia-induced pulmonary hypertension in mice. Arterioscler Thromb Vasc Biol. 2013;33:2780–91.
pubmed: 24135024
doi: 10.1161/ATVBAHA.113.301357
Hartmann S, Ridley AJ, Lutz S. The Function of Rho-Associated kinases ROCK1 and ROCK2 in the pathogenesis of cardiovascular disease. Front Pharm. 2015;6:276.
doi: 10.3389/fphar.2015.00276
Strassheim D, Gerasimovskaya E, Irwin D, Dempsey EC, Stenmark K, Karoor V. RhoGTPase in vascular disease. Cells. 2019;8:551.
pmcid: 6627336
doi: 10.3390/cells8060551
Scruggs SB, Hinken AC, Thawornkaiwong A, Robbins J, Walker LA, de Tombe PP, et al. Ablation of ventricular myosin regulatory light chain phosphorylation in mice causes cardiac dysfunction in situ and affects neighboring myofilament protein phosphorylation. J Biol Chem. 2009;284:5097–106.
pubmed: 19106098
pmcid: 2643522
doi: 10.1074/jbc.M807414200
Ding P, Huang J, Battiprolu PK, Hill JA, Kamm KE, Stull JT. Cardiac myosin light chain kinase is necessary for myosin regulatory light chain phosphorylation and cardiac performance in vivo. J Biol Chem. 2010;285:40819–29.
pubmed: 20943660
pmcid: 3003383
doi: 10.1074/jbc.M110.160499
Warren SA, Briggs LE, Zeng H, Chuang J, Chang EI, Terada R, et al. Myosin light chain phosphorylation is critical for adaptation to cardiac stress. Circulation. 2012;126:2575–88.
pubmed: 23095280
pmcid: 3510779
doi: 10.1161/CIRCULATIONAHA.112.116202
Chang AN, Battiprolu PK, Cowley PM, Chen G, Gerard RD, Pinto JR, et al. Constitutive phosphorylation of cardiac myosin regulatory light chain in vivo. J Biol Chem. 2015;290:10703–16.
pubmed: 25733667
pmcid: 4409237
doi: 10.1074/jbc.M115.642165
Andersen GØ, Qvigstad E, Schiander I, Aass H, Osnes JB, Skomedal T. α1-AR-induced positive inotropic response in heart is dependent on myosin light chain phosphorylation. Am J Physiol Heart Circ Physiol. 2002;283:H1471–80.
pubmed: 12234799
doi: 10.1152/ajpheart.00232.2002
Riise J, Nguyen CH, Qvigstad E, Sandnes DL, Osnes JB, Skomedal T, et al. Prostanoid F receptors elicit an inotropic effect in rat left ventricle by enhancing myosin light chain phosphorylation. Cardiovasc Res. 2008;80:407–15.
pubmed: 18703533
doi: 10.1093/cvr/cvn216
Davis JS, Hassanzadeh S, Winitsky S, Lin H, Satorius C, Vemuri R, et al. The overall pattern of cardiac contraction depends on a spatial gradient of myosin regulatory light chain phosphorylation. Cell. 2001;107:631–41.
pubmed: 11733062
doi: 10.1016/S0092-8674(01)00586-4
Seguchi O, Takashima S, Yamazaki S, Asakura M, Asano Y, Shintani Y, et al. A cardiac myosin light chain kinase regulates sarcomere assembly in the vertebrate heart. J Clin Invest. 2007;117:2812–24.
pubmed: 17885681
pmcid: 1978424
doi: 10.1172/JCI30804
Chan JY, Takeda M, Briggs LE, Graham ML, Lu JT, Horikoshi N, et al. Identification of cardiac-specific myosin light chain kinase. Circ Res. 2008;102:571–80.
pubmed: 18202317
pmcid: 2504503
doi: 10.1161/CIRCRESAHA.107.161687
Chang AN, Mahajan P, Knapp S, Barton H, Sweeney HL, Kamm KE, et al. Cardiac myosin light chain is phosphorylated by Ca
pubmed: 27325775
pmcid: 4941474
doi: 10.1073/pnas.1600633113
Taniguchi M, Okamoto R, Ito M, Goto I, Fujita S, Konishi K, et al. New isoform of cardiac myosin light chain kinase and the role of cardiac myosin phosphorylation in α
pubmed: 26512720
pmcid: 4626101
doi: 10.1371/journal.pone.0141130
Sevrieva IR, Brandmeier B, Ponnam S, Gautel M, Irving M, Campbell KS, et al. Cardiac myosin regulatory light chain kinase modulates cardiac contractility by phosphorylating both myosin regulatory light chain and troponin I. J Biol Chem. 2020;295:4398–410.
pubmed: 32086378
pmcid: 7135997
doi: 10.1074/jbc.RA119.011945
Liu R, Correll RN, Davis J, Vagnozzi RJ, York AJ, Sargent MA, et al. Cardiac-specific deletion of protein phosphatase 1β promotes increased myofilament protein phosphorylation and contractile alterations. J Mol Cell Cardiol. 2015;87:204–13.
pubmed: 26334248
pmcid: 4637224
doi: 10.1016/j.yjmcc.2015.08.018
Fujioka M, Takahashi N, Odai H, Araki S, Ichikawa K, Feng J, et al. A new isoform of human myosin phosphatase targeting/regulatory subunit (MYPT2): cDNA cloning, tissue expression, and chromosomal mapping. Genomics. 1998;49:59–68.
pubmed: 9570949
doi: 10.1006/geno.1998.5222
Moorhead G, Johnson D, Morrice N, Cohen P. The major myosin phosphatase in skeletal muscle is a complex between the β-isoform of protein phosphatase 1 and the MYPT2 gene product. FEBS Lett. 1998;438:141–4.
pubmed: 9827534
doi: 10.1016/S0014-5793(98)01276-9
Arimura T, Suematsu N, Zhou YB, Nishimura J, Satoh S, Takeshita A, et al. Identification, characterization, and functional analysis of heart-specific myosin light chain phosphatase small subunit. J Biol Chem. 2001;276:6073–82.
pubmed: 11067852
doi: 10.1074/jbc.M008566200
Okamoto R, Kato T, Mizoguchi A, Takahashi N, Nakakuki T, Mizutani H, et al. Characterization and function of MYPT2, a target subunit of myosin phosphatase in heart. Cell Signal. 2006;18:1408–16.
pubmed: 16431080
doi: 10.1016/j.cellsig.2005.11.001
Morano I, Hofmann F, Zimmer M, Rüegg JC. The influence of P-light chain phosphorylation by myosin light chain kinase on the calcium sensitivity of chemically skinned heart fibres. FEBS Lett. 1985;189:221–4.
pubmed: 3840099
doi: 10.1016/0014-5793(85)81027-9
Sweeney HL, Stull JT. Phosphorylation of myosin in permeabilized mammalian cardiac and skeletal muscle cells. Am J Physiol. 1986;250:C657–60.
pubmed: 3754389
doi: 10.1152/ajpcell.1986.250.4.C657
Olsson MC, Patel JR, Fitzsimons DP, Walker JW, Moss RL. Basal myosin light chain phosphorylation is a determinant of Ca
pubmed: 15331360
doi: 10.1152/ajpheart.01067.2003
Stelzer JE, Patel JR, Moss RL. Acceleration of stretch activation in murine myocardium due to phosphorylation of myosin regulatory light chain. J Gen Physiol. 2006;128:261–72.
pubmed: 16908724
pmcid: 2151564
doi: 10.1085/jgp.200609547
Kampourakis T, Sun YB, Irving M. Myosin light chain phosphorylation enhances contraction of heart muscle via structural changes in both thick and thin filaments. Proc Natl Acad Sci USA. 2016;113:E3039–47.
pubmed: 27162358
pmcid: 4889392
doi: 10.1073/pnas.1602776113
Sheikh F, Ouyang K, Campbell SG, Lyon RC, Chuang J, Fitzsimons D, et al. Mouse and computational models link Mlc2v dephosphorylation to altered myosin kinetics in early cardiac disease. J Clin Invest. 2012;122:1209–21.
pubmed: 22426213
pmcid: 3314469
doi: 10.1172/JCI61134
van der Velden J, Papp Z, Zaremba R, Boontje NM, de Jong JW, Owen VJ, et al. Increased Ca
pubmed: 12504812
doi: 10.1016/S0008-6363(02)00606-5
van der Velden J, Papp Z, Boontje NM, Zaremba R, de Jong JW, Janssen PM, et al. The effect of myosin light chain 2 dephosphorylation on Ca
pubmed: 12566123
doi: 10.1016/S0008-6363(02)00662-4
Riise J, Nguyen CH, Hussain RI, Dahl CP, Ege MS, Osnes JB, et al. Prostanoid-mediated inotropic responses are attenuated in failing human and rat ventricular myocardium. Eur J Pharm. 2012;686:66–73.
doi: 10.1016/j.ejphar.2012.04.022
Aoki H, Sadoshima J, Izumo S. Myosin light chain kinase mediates sarcomere organization during cardiac hypertrophy in vitro. Nat Med. 2000;6:183–8.
pubmed: 10655107
doi: 10.1038/72287
Wang S, Cheng M, Hu Z, Hu S, Zou Q, Lai X, et al. Angiotensin II facilitates matrix metalloproteinase-9-mediated myosin light chain kinase degradation in pressure overload-induced cardiac hypertrophy. Cell Physiol Biochem. 2017;44:2281–95.
pubmed: 29262413
doi: 10.1159/000486066
Wang S, Wang H, Su X, Liu B, Wang L, Yan H, et al. β-adrenergic activation may promote myosin light chain kinase degradation through calpain in pressure overload-induced cardiac hypertrophy: β-adrenergic activation results in MLCK degradation. Biomed Pharmacother. 2020;129:110438.
pubmed: 32768940
doi: 10.1016/j.biopha.2020.110438
Poetter K, Jiang H, Hassanzadeh S, Master SR, Chang A, Dalakas MC, et al. Mutations in either the essential or regulatory light chains of myosin are associated with a rare myopathy in human heart and skeletal muscle. Nat Genet. 1996;13:63–9.
pubmed: 8673105
doi: 10.1038/ng0596-63
Andersen PS, Havndrup O, Bundgaard H, Moolman-Smook JC, Larsen LA, Mogensen J, et al. Myosin light chain mutations in familial hypertrophic cardiomyopathy: phenotypic presentation and frequency in Danish and South African populations. J Med Genet. 2001;38:e43.
pubmed: 11748309
pmcid: 1734772
doi: 10.1136/jmg.38.12.e43
Richard P, Charron P, Carrier L, Ledeuil C, Cheav T, Pichereau C, et al. Hypertrophic cardiomyopathy: Distribution of disease genes, spectrum of mutations, and implications for a molecular diagnosis strategy. Circulation. 2003;107:2227–32.
pubmed: 12707239
doi: 10.1161/01.CIR.0000066323.15244.54
Szczesna-Cordary D, Guzman G, Zhao J, Hernandez O, Wei J, Diaz-Perez Z. The E22K mutation of myosin RLC that causes familial hypertrophic cardiomyopathy increases calcium sensitivity of force and ATPase in transgenic mice. J Cell Sci. 2005;118:3675–83.
pubmed: 16076902
doi: 10.1242/jcs.02492
Yadav S, Szczesna-Cordary D. Pseudophosphorylation of cardiac myosin regulatory light chain: a promising new tool for treatment of cardiomyopathy. Biophys Rev. 2017;9:57–64.
pubmed: 28510043
pmcid: 5418495
doi: 10.1007/s12551-017-0248-8
Tobita T, Nomura S, Morita H, Ko T, Fujita T, Toko H, et al. Identification of MYLK3 mutations in familial dilated cardiomyopathy. Sci Rep. 2017;7:17495.
pubmed: 29235529
pmcid: 5727479
doi: 10.1038/s41598-017-17769-1
Hodatsu A, Fujino N, Uyama Y, Tsukamoto O, Imai-Okazaki A, Yamazaki S, et al. Impact of cardiac myosin light chain kinase gene mutation on development of dilated cardiomyopathy. ESC Heart Fail. 2019;6:406–15.
pubmed: 30690923
pmcid: 6437445
doi: 10.1002/ehf2.12410
Mizutani H, Okamoto R, Moriki N, Konishi K, Taniguchi M, Fujita S, et al. Overexpression of myosin phosphatase reduces Ca
pubmed: 19966500
doi: 10.1253/circj.CJ-09-0462
Tan I, Ng CH, Lim L, Leung T. Phosphorylation of a novel myosin binding subunit of protein phosphatase 1 reveals a conserved mechanism in the regulation of actin cytoskeleton. J Biol Chem. 2001;276:21209–16.
pubmed: 11399775
doi: 10.1074/jbc.M102615200