Ca
ATG9A
Calcium
Calreticulin
Lysine acetylation
Proteostasis
Reticulophagy
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
26 Oct 2024
26 Oct 2024
Historique:
received:
22
08
2024
accepted:
17
10
2024
medline:
27
10
2024
pubmed:
27
10
2024
entrez:
27
10
2024
Statut:
epublish
Résumé
The acetylation of autophagy protein 9 A (ATG9A) in the lumen of the endoplasmic reticulum (ER) by ATase1 and ATase2 regulates the induction of reticulophagy. Analysis of the ER-specific ATG9A interactome identified calreticulin (CALR), an ER luminal Ca
Identifiants
pubmed: 39462136
doi: 10.1038/s41598-024-76854-4
pii: 10.1038/s41598-024-76854-4
doi:
Substances chimiques
Calreticulin
0
Autophagy-Related Proteins
0
Calcium
SY7Q814VUP
Membrane Proteins
0
Lysine
K3Z4F929H6
Vesicular Transport Proteins
0
ATG9A protein, human
0
CALR protein, human
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
25532Subventions
Organisme : NINDS NIH HHS
ID : NS094154
Pays : United States
Organisme : NIGMS NIH HHS
ID : GM148487
Pays : United States
Organisme : NIA NIH HHS
ID : AG078794
Pays : United States
Informations de copyright
© 2024. The Author(s).
Références
Fernandez-Fuente, G., Rigby, M. J. & Puglielli, L. Intracellular citrate/acetyl-CoA flux and endoplasmic reticulum acetylation: Connectivity is the answer. Mol. Metab.67, 101653. https://doi.org/10.1016/j.molmet.2022.101653 (2023).
doi: 10.1016/j.molmet.2022.101653
pubmed: 36513219
Nieborak, A. & Schneider, R. Metabolic intermediates - cellular messengers talking to chromatin modifiers. Mol. Metab.14, 39–52. https://doi.org/10.1016/j.molmet.2018.01.007 (2018).
doi: 10.1016/j.molmet.2018.01.007
pubmed: 29397344
pmcid: 6034042
Kaelin, W. G. Jr & McKnight, S. L. Influence of metabolism on epigenetics and disease. Cell153, 56–69. https://doi.org/10.1016/j.cell.2013.03.004 (2013).
doi: 10.1016/j.cell.2013.03.004
pubmed: 23540690
pmcid: 3775362
Pehar, M., Jonas, M. C., Hare, T. M. & Puglielli, L. SLC33A1/AT-1 protein regulates the induction of autophagy downstream of IRE1/XBP1 pathway. J. Biol. Chem.287, 29921–29930. https://doi.org/10.1074/jbc.M112.363911 (2012).
doi: 10.1074/jbc.M112.363911
pubmed: 22787145
pmcid: 3436137
Peng, Y. et al. Deficient import of Acetyl-CoA into the ER lumen causes neurodegeneration and propensity to infections, inflammation, and Cancer. J. Neurosci.34, 6772–6789. https://doi.org/10.1523/JNEUROSCI.0077-14.2014 (2014).
doi: 10.1523/JNEUROSCI.0077-14.2014
pubmed: 24828632
pmcid: 4019794
Peng, Y. et al. Increased transport of acetyl-CoA into the endoplasmic reticulum causes a progeria-like phenotype. Aging Cell. e12820. https://doi.org/10.1111/acel.12820 (2018).
Rigby, M. J. et al. Endoplasmic reticulum acetyltransferases Atase1 and Atase2 differentially regulate reticulophagy, macroautophagy and cellular acetyl-CoA metabolism. Commun. Biol.4, 454. https://doi.org/10.1038/s42003-021-01992-8 (2021).
doi: 10.1038/s42003-021-01992-8
pubmed: 33846551
pmcid: 8041774
Fernandez-Fuente, G. et al. The citrate transporters SLC13A5 and SLC25A1 elicit different metabolic responses and phenotypes in the mouse. Commun. Biol.6, 926. https://doi.org/10.1038/s42003-023-05311-1 (2023).
doi: 10.1038/s42003-023-05311-1
pubmed: 37689798
pmcid: 10492862
Peng, Y. et al. Improved proteostasis in the secretory pathway rescues Alzheimer’s disease in the mouse. Brain. 139, 937–952. https://doi.org/10.1093/brain/awv385 (2016).
doi: 10.1093/brain/awv385
pubmed: 26787453
pmcid: 4805081
Murie, M. et al. ATase inhibition rescues age-associated proteotoxicity of the secretory pathway. Commun. Biol.5, 173. https://doi.org/10.1038/s42003-022-03118-0 (2022).
doi: 10.1038/s42003-022-03118-0
pubmed: 35217767
pmcid: 8881600
Hullinger, R. et al. Increased expression of AT-1/SLC33A1 causes an autistic-like phenotype in mice by affecting dendritic branching and spine formation. J. Exp. Med.213, 1267–1284. https://doi.org/10.1084/jem.20151776 (2016).
doi: 10.1084/jem.20151776
pubmed: 27242167
pmcid: 4925020
Rigby, M. J. et al. Increased expression of SLC25A1/CIC causes an autistic-like phenotype with altered neuron morphology. Brain https://doi.org/10.1093/brain/awab295 (2022).
doi: 10.1093/brain/awab295
pubmed: 35203088
pmcid: 9014753
Rigby, M. J. et al. SLC13A5/sodium-citrate co-transporter overexpression causes disrupted white matter integrity and an autistic-like phenotype. Brain Commun.4, fcac002. https://doi.org/10.1093/braincomms/fcac002 (2022).
doi: 10.1093/braincomms/fcac002
pubmed: 35146426
pmcid: 8823335
Sheehan, B. K., Orefice, N. S., Peng, Y., Shapiro, S. L. & Puglielli, L. ATG9A regulates proteostasis through reticulophagy receptors FAM134B and SEC62 and folding chaperones CALR and HSPB1. iScience24, 102315. https://doi.org/10.1016/j.isci.2021.102315 (2021).
Liang, J. R., Lingeman, E., Ahmed, S. & Corn, J. E. Atlastins remodel the endoplasmic reticulum for selective autophagy. J. Cell. Biol.217, 3354–3367. https://doi.org/10.1083/jcb.201804185 (2018).
doi: 10.1083/jcb.201804185
pubmed: 30143524
pmcid: 6168278
Daverkausen-Fischer, L. & Prols, F. Regulation of calcium homeostasis and flux between the endoplasmic reticulum and the cytosol. J. Biol. Chem.298, 102061. https://doi.org/10.1016/j.jbc.2022.102061 (2022).
doi: 10.1016/j.jbc.2022.102061
pubmed: 35609712
pmcid: 9218512
Engedal, N. et al. Modulation of intracellular calcium homeostasis blocks autophagosome formation. Autophagy9, 1475–1490. https://doi.org/10.4161/auto.25900 (2013).
doi: 10.4161/auto.25900
pubmed: 23970164
Villamil Giraldo, A. M. et al. The structure of calreticulin C-terminal domain is modulated by physiological variations of calcium concentration. J. Biol. Chem.285, 4544–4553. https://doi.org/10.1074/jbc.M109.034512 (2010).
doi: 10.1074/jbc.M109.034512
pubmed: 20018892
Young, A. R. et al. Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes. J. Cell. Sci.119, 3888–3900 (2006).
doi: 10.1242/jcs.03172
pubmed: 16940348
Tamura, H., Shibata, M., Koike, M., Sasaki, M. & Uchiyama, Y. Atg9A protein, an autophagy-related membrane protein, is localized in the neurons of mouse brains. J. Histochem. Cytochem.58, 443–453 (2010).
doi: 10.1369/jhc.2010.955690
pubmed: 20124090
pmcid: 2857816
Ohashi, Y. & Munro, S. Membrane delivery to the yeast autophagosome from the golgi-endosomal system. Mol. Biol. Cell.21, 3998–4008 (2010).
doi: 10.1091/mbc.e10-05-0457
pubmed: 20861302
pmcid: 2982105
Puri, C., Renna, M., Bento, C. F., Moreau, K. & Rubinsztein, D. C. Diverse autophagosome membrane sources coalesce in recycling endosomes. Cell154, 1285–1299. https://doi.org/10.1016/j.cell.2013.08.044 (2013).
doi: 10.1016/j.cell.2013.08.044
pubmed: 24034251
pmcid: 3791395
Bejarano, E. et al. Connexins modulate autophagosome biogenesis. Nat. Cell. Biol.16, 401–414. https://doi.org/10.1038/ncb2934 (2014).
doi: 10.1038/ncb2934
pubmed: 24705551
pmcid: 4008708
Saitoh, T. et al. Atg9a controls dsDNA-driven dynamic translocation of STING and the innate immune response. Proc. Natl. Acad. Sci. USA106, 20842–20846. https://doi.org/10.1073/pnas.0911267106 (2009).
doi: 10.1073/pnas.0911267106
pubmed: 19926846
pmcid: 2791563
Sawa-Makarska, J. et al. Reconstitution of autophagosome nucleation defines Atg9 vesicles as seeds for membrane formation. Science369 https://doi.org/10.1126/science.aaz7714 (2020).
Claude-Taupin, A. et al. ATG9A protects the plasma membrane from programmed and incidental permeabilization. Nat. Cell. Biol.23, 846–858. https://doi.org/10.1038/s41556-021-00706-w (2021).
doi: 10.1038/s41556-021-00706-w
pubmed: 34257406
pmcid: 8276549
van Vliet, A. R. et al. Exploring the ATG9A interactome uncovers interaction with VPS13A. J. Cell. Sci.137 https://doi.org/10.1242/jcs.261081 (2024).
Carreras-Sureda, A., Pihan, P. & Hetz, C. Calcium signaling at the endoplasmic reticulum: Fine-tuning stress responses. Cell. Calcium70, 24–31. https://doi.org/10.1016/j.ceca.2017.08.004 (2018).
doi: 10.1016/j.ceca.2017.08.004
pubmed: 29054537
Guardia, C. M. et al. Structure of human ATG9A, the only transmembrane protein of the core autophagy machinery. Cell. Rep.31, 107837. https://doi.org/10.1016/j.celrep.2020.107837 (2020).
doi: 10.1016/j.celrep.2020.107837
pubmed: 32610138
pmcid: 7388177
Lai, L. T. F. et al. Subnanometer resolution cryo-EM structure of Arabidopsis thaliana ATG9. Autophagy16, 575–583. https://doi.org/10.1080/15548627.2019.1639300 (2020).
doi: 10.1080/15548627.2019.1639300
pubmed: 31276439
Maeda, S. et al. Structure, lipid scrambling activity and role in autophagosome formation of ATG9A. Nat. Struct. Mol. Biol.27 https://doi.org/10.1038/s41594-020-00520-2 (2020).
Matoba, K. et al. Atg9 is a lipid scramblase that mediates autophagosomal membrane expansion. Nat. Struct. Mol. Biol.27 https://doi.org/10.1038/s41594-020-00518-w (2020).
Dieterich, I. A. et al. Acetyl-CoA flux from the cytosol to the ER regulates engagement and quality of the secretory pathway. Sci. Rep.11, 2013. https://doi.org/10.1038/s41598-021-81447-6 (2021).
doi: 10.1038/s41598-021-81447-6
pubmed: 33479349
pmcid: 7820588
Ding, Y. et al. Biochemical inhibition of the acetyltansferases ATase1 and ATase2 reduces b-secretase (BACE1) levels and ab generation. J. Biol. Chem.287, 8424–8433 (2012).
doi: 10.1074/jbc.M111.310136
pubmed: 22267734
pmcid: 3318698