Cytoskeletal protein Zyxin in embryonic development: from controlling cell movements and pluripotency to regulating embryonic patterning.
development
differentiation
morphogenesis
pluripotency
protein interactions
transcription factor
zyxin
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
01 2023
01 2023
Historique:
revised:
29
09
2021
received:
30
06
2021
accepted:
30
11
2021
pubmed:
3
12
2021
medline:
6
1
2023
entrez:
2
12
2021
Statut:
ppublish
Résumé
The Lim-domain protein Zyxin was initially identified as a minor actin cytoskeleton protein that regulates the assembly and repair of actin filaments. At the same time, additional functions revealed for Zyxin in recent decades indicate that this protein can also play an important role in regulating gene expression and cell differentiation. In this review, we analysed the data in the literature pointing to Zyxin as one of the possible molecular hubs linking morphogenetic cell movements with gene expression, stem cell status regulation and pattern formation during the most complex processes in organism life, embryogenesis.
Substances chimiques
Zyxin
0
Cytoskeletal Proteins
0
Types de publication
Review
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
66-72Informations de copyright
© 2021 Federation of European Biochemical Societies.
Références
Smith MA, Hoffman LM & Beckerle MC (2014) LIM proteins in actin cytoskeleton mechanoresponse. Trends Cell Biol 24, 575-583.
Hervy M, Hoffman L & Beckerle MC (2006) From the membrane to the nucleus and back again: bifunctional focal adhesion proteins. Curr Opin Cell Biol 18, 524-532.
Wang YX, Wang DY, Guo YC & Guo J (2019) Zyxin: a mechanotransductor to regulate gene expression. Eur Rev Med Pharmacol Sci 23, 413-425.
Sabino F, Madzharova E & Auf dem Keller U (2020) Cell density-dependent proteolysis by HtrA1 induces translocation of Zyxin to the nucleus and increased cell survival. Cell Death Dis 11, 674.
Wang Y & Gilmore TD (2003) Zyxin and paxillin proteins: focal adhesion plaque LIM domain proteins go nuclear. Biochim Biophys Acta 1593, 115-120.
Wu C (2007) Focal adhesion: a focal point in current cell biology and molecular medicine. Cell Adh Migr 1, 13-18.
Nix DA, Fradelizi J, Bockholt S, Menichi B, Louvard D, Friederich E & Beckerle MC (2001) Targeting of Zyxin to sites of actin membrane interaction and to the nucleus. J Biol Chem 276, 34759-34767.
Martynova NY, Parshina EA, Ermolina LV & Zaraisky AG (2018) The cytoskeletal protein Zyxin interacts with the zinc-finger transcription factor Zic1 and plays the role of a scaffold for Gli1 and Zic1 interactions during early development of Xenopus laevis. Biochem Biophys Res Commun 504, 251-256.
Cattaruzza M, Lattrich C & Hecker M (2004) Focal adhesion protein Zyxin is a mechanosensitive modulator of gene expression in vascular smooth muscle cells. Hypertension 43, 726-730.
Suresh Babu S, Wojtowicz A, Freichel M, Birnbaumer L, Hecker M & Cattaruzza M (2012) Mechanism of stretch-induced activation of the mechanotransducer Zyxin in vascular cells. Sci Signal 5, 91.
Fujita Y, Yamaguchi A, Hata K, Endo M, Yamaguchi N & Yamashita T (2009) Zyxin is a novel interacting partner for SIRT1. BMC Cell Biol 10, 6.
Hervy M, Hoffman LM, Jensen CC, Smith M & Beckerle MC (2010) The LIM protein Zyxin binds CARP-1 and promotes apoptosis. Genes Cancer 1, 506-515.
Tamura R, Jiang F, Xie J & Kamiyama D (2021) Multiplexed labeling of cellular proteins with split fluorescent protein tags. Commun Biol 4, 257.
Sun X, Phua DYZ, Axiotakis L, Smith MA, Blankman E, Gong R, Cail RC, Espinosa de los Reyes S, Beckerle MC, Waterman CM et al. (2020) Mechanosensing through direct binding of tensed F-actin by LIM domains. Dev Cell 55, 468-482.
Winkelman JD, Anderson CA, Suarez C, Kovar DR & Gardel ML (2020) Evolutionarily diverse LIM domain-containing proteins bind stressed actin filaments through a conserved mechanism. Proc Natl Acad Sci USA 117, 25532-25542.
Moody JD, Grange J, Ascione MP, Boothe D & BushnellE HMD (2009) A Zyxin head-tail interaction regulates Zyxin-VASP complex formation. Biochem Biophys Res Commun 378, 625-628.
Call GS, Chung JY, Davis JA, Price BD, Primavera TS, Thomson NC, Wagner MV & Hansen MD (2011) Zyxin phosphorylation at serine 142 modulates the Zyxin head-tail interaction to alter cell-cell adhesion. Biochem Biophys Res Commun 404, 780-784.
Oku S, Takahashi N, Fukata Y & Fukata M (2013) In silico screening for palmitoyl substrates reveals a role for DHHC1/3/10 (zDHHC1/3/11)-mediated neurochondrin palmitoylation in its targeting to Rab5-positive endosomes. J Biol Chem 288, 19816-19829.
Martynova NY, Parshina EA & Zaraisky AG (2021) Protocol for separation of the nuclear and the cytoplasmic fractions of Xenopus laevis embryonic cells for studying protein shuttling. STAR Protoc 2, 100449.
Ma B, Cheng H, Gao R, Mu C, Chen L, Wu S, Chen Q & Zhu Y (2016) Zyxin-Siah2-Lats2 axis mediates cooperation between Hippo and TGF-β signalling pathways. Nat Commun 7, 11123.
Martynova N, Ermolina L, Ermakova G, Eroshkin F, Gyoeva F, Baturina N & Zaraisky A (2013) The cytoskeletal protein Zyxin inhibits Shh signaling during the CNS patterning in Xenopus laevis through interaction with the transcription factor Gli1. Dev Biol 380, 37-48.
Li N, Goodwin RL & Potts JD (2013) Zyxin regulates cell migration and differentiation in EMT during chicken AV valve morphogenesis. Microsc Microanal 19, 842-854.
Hoffman LM, Nix DA, Benson B, Boot-Hanford R, Gustafsson E, Jamora C, Menzies AS, Goh KL, Jensen CC, Gertler FB et al. (2003) Targeted disruption of the murine zyxin gene. Mol Cell Biol 23, 70-79.
Rossi A, Kontarakis Z, Gerri C, Nolte H, Hölper S, Krüger M & Stainier DY (2015) Genetic compensation induced by deleterious mutations but not gene knockdowns. Nature 524, 230-233.
Luo S, Schaefer AM, Dour S & Nonet ML (2014) The conserved LIM domain-containing focal adhesion protein ZYX-1 regulates synapse maintenance in Caenorhabditis elegans. Development 141, 3922-3933.
Renfranz PJ, Blankman E & Beckerle MC (2010) The cytoskeletal regulator zyxin is required for viability in Drosophila melanogaster. Anat Rec 293, 1455-1469.
Rausch V & Hansen CG (2020) The hippo pathway, YAP/TAZ, and the plasma membrane. Trends Cell Biol 30, 32-48.
Dasgupta I & McCollum D (2019) Control of cellular responses to mechanical cues through YAP/TAZ regulation. J Biol Chem 294(46), 17693-17706.
Rauskolb C, Pan G, Reddy BV, Oh H & Irvine KD (2011) Zyxin links fat signaling to the hippo pathway. PLoS Biol 9, e1000624.
Gaspar P, Holder MV, Aerne BL & JanodyF TN (2015) Zyxin antagonises the FERM protein expanded to couple F-actin and Yorkie-dependent organ growth. Curr Biol 25, 679-689.
Martynova N, Ermolina L, Eroshkin F, Gioeva F & Zaraĭsky A (2008) Transcriptional factor Xanf1 interacts with the focal adhesion protein Zyxin in the early development of the Xenopus laevis brain. Bioorg Khim 34, 573-576.
Zaraisky AG, Lukyanov SA, Vasiliev OL, Smirnov YV, Belyavsky AV & Kazanskaya OV (1992) A novel homeobox gene expressed in the anterior neural plate of the Xenopus embryo. Dev Biol 152, 373-382.
Ermakova GV, Alexandrova EM, Kazanskaya OV, Vasiliev OL, Smith MW & Zaraisky AG (1999) The homeobox gene, Xanf-1, can control both neural differentiation and patterning in the presumptive anterior neurectoderm of the Xenopus laevis embryo. Development 126, 4513-4523.
Kazanskaya OV, Severtzova EA, Barth KA, Ermakova GV, Lukyanov SA, Benyumov AO, Pannese M, Boncinelli E, Wilson SW & Zaraisky AG (1997) Anf: a novel class of vertebrate homeobox genes expressed at the anterior end of the main embryonic axis. Gene 200, 25-34.
Bayramov AV, Ermakova GV, Eroshkin FM, Kucheryavyy AV, Martynova NY & Zaraisky AG (2016) The presence of Anf/Hesx1 homeobox gene in lampreys suggests that it could play an important role in emergence of telencephalon. Sci Rep 6, 39849.
Ermakova GV, Solovieva EA, Martynova NY & Zaraisky AG (2007) The homeodomain factor Xanf represses expression of genes in the presumptive rostral forebrain that specify more caudal brain regions. Dev Biol 307, 483-497.
Martynova NY, Eroshkin FM, Ermolina LV, Ermakova GV, Korotaeva AL, Smurova KM, Gyoeva FK & Zaraisky AG (2008) The LIM-domain protein Zyxin binds the homeodomain factor Xanf1/Hesx1 and modulates its activity in the anterior neural plate of Xenopus laevis embryo. Dev Dyn 237, 736-749.
Martynova NU, Ermolina LV, Eroshkin FM & Zarayskiy AG (2015) The cytoskelrtal protein zyxin interacts with the hedgehog receptor patched. Bioorg Khim 41, 744-748.
Koyabu Y, Nakata K, Mizugishi K, Aruga J & Mikoshiba K (2001) Physical and functional interactions between Zic and Gli proteins. J Biol Chem 276(10), 6889-6892.
Kohli P, Höhne M, Jüngst C, Bertsch S, Ebert LK, Schauss AC, Benzing T, Rinschen MM & Schermer B (2017) The ciliary membrane-associated proteome reveals actin-binding proteins as key components of cilia. EMBO Rep 18, 1521-1535.
Shukla S, Urbanek P, Frappart L, Hänold R, Nagel S, Monajembashi S, Grigaravicius P, Min WK, Tapias A, Kassel O, Heuer H, Wang Z, Ploubidou A & Herrlich P (2019) Novel function of TRIP6, in brain ciliogenesis. bioRxiv https://doi.org/https://doi.org/10.1101/777052.
Wheway G, Nazlamova L & Hancock J (2018) Signaling through the Primary Cilium. Front Cell Dev Biol 6, doi: 10.3389/fcell.2018.00008
Tukachinsky H, Lopez LV & Salic A (2010) A mechanism for vertebrate Hedgehog signaling: recruitment to cilia and dissociation of SuFu-Gli protein complexes. J Cell Biol 191, 415-428.
Parshina EA, Eroshkin FM, Оrlov EE, Gyoeva FK, Shokhina AG, Staroverov DB, Belousov VV, Zhigalova NA, Prokhortchouk EB, Zaraisky AG et al. (2020) Cytoskeletal protein zyxin inhibits the activity of genes responsible for embryonic stem cell status. Cell Rep 33(7), 108396. doi: 10.1016/j.celrep.2020.108396
Eliseeva IA, Kim ER, Guryanov SG, Ovchinnikov LP & Lyabin DN (2011) Y-box-binding protein 1 (YB-1) and its functions. Biochemistry 76, 1402-1433.
Han J, Liu G, Profirovic J, Niu J & Voyno-Yasenetskaya T (2009) Zyxin is involved in thrombin signaling via interaction with PAR-1 receptor. FASEB J 23, 4193-4206.