{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T12:28:56Z","timestamp":1770726536565,"version":"3.49.0"},"reference-count":63,"publisher":"MDPI AG","issue":"24","license":[{"start":{"date-parts":[[2020,12,16]],"date-time":"2020-12-16T00:00:00Z","timestamp":1608076800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003448","name":"General Secretariat for Research and Technology","doi-asserted-by":"publisher","award":["MIS 5002802"],"award-info":[{"award-number":["MIS 5002802"]}],"id":[{"id":"10.13039\/501100003448","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001674","name":"Fondation Leducq","doi-asserted-by":"publisher","award":["CURE-PLaN"],"award-info":[{"award-number":["CURE-PLaN"]}],"id":[{"id":"10.13039\/501100001674","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The cytoskeleton has a primary role in cardiomyocyte function, including the response to mechanical stimuli and injury. The small heat shock protein 20 (Hsp20) conveys protective effects in cardiac muscle that are linked to serine-16 (Ser16) Hsp20 phosphorylation by stress-induced PKA, but the link between Hsp20 and the cytoskeleton remains poorly understood. Herein, we demonstrate a physical and functional interaction of Hsp20 with the cytoskeletal protein 14-3-3. We show that, upon phosphorylation at Ser16, Hsp20 translocates from the cytosol to the cytoskeleton where it binds to 14-3-3. This leads to dissociation of 14-3-3 from the F-actin depolymerization regulator cofilin-2 (CFL2) and enhanced F-actin depolymerization. Importantly, we demonstrate that the P20L Hsp20 mutation associated with dilated cardiomyopathy exhibits reduced physical interaction with 14-3-3 due to diminished Ser16 phosphorylation, with subsequent failure to translocate to the cytoskeleton and inability to disassemble the 14-3-3\/CFL2 complex. The topological sequestration of Hsp20 P20L ultimately results in impaired regulation of F-actin dynamics, an effect implicated in loss of cytoskeletal integrity and amelioration of the cardioprotective functions of Hsp20. These findings underscore the significance of Hsp20 phosphorylation in the regulation of actin cytoskeleton dynamics, with important implications in cardiac muscle physiology and pathophysiology.<\/jats:p>","DOI":"10.3390\/ijms21249572","type":"journal-article","created":{"date-parts":[[2020,12,16]],"date-time":"2020-12-16T09:21:15Z","timestamp":1608110475000},"page":"9572","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["The Cardioprotective PKA-Mediated Hsp20 Phosphorylation Modulates Protein Associations Regulating Cytoskeletal Dynamics"],"prefix":"10.3390","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9931-7099","authenticated-orcid":false,"given":"Elizabeth","family":"Vafiadaki","sequence":"first","affiliation":[{"name":"Molecular Biology Division, Biomedical Research Foundation of the Academy of Athens, 115 27 Athens, Greece"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1231-320X","authenticated-orcid":false,"given":"Demetrios A.","family":"Arvanitis","sequence":"additional","affiliation":[{"name":"Molecular Biology Division, Biomedical Research Foundation of the Academy of Athens, 115 27 Athens, Greece"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6403-6761","authenticated-orcid":false,"given":"Aristides G.","family":"Eliopoulos","sequence":"additional","affiliation":[{"name":"Molecular Biology Division, Biomedical Research Foundation of the Academy of Athens, 115 27 Athens, Greece"},{"name":"Department of Biology, School of Medicine, National and Kapodistrian University of Athens, 115 27 Athens, Greece"},{"name":"Center for New Biotechnologies and Precision Medicine, Medical School, National and Kapodistrian University of Athens, 115 27 Athens, Greece"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Evangelia G.","family":"Kranias","sequence":"additional","affiliation":[{"name":"Molecular Biology Division, Biomedical Research Foundation of the Academy of Athens, 115 27 Athens, Greece"},{"name":"Department of Pharmacology and Systems Physiology, University of Cincinnati, College of Medicine, Cincinnati, OH 45267-0575, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3704-1941","authenticated-orcid":false,"given":"Despina","family":"Sanoudou","sequence":"additional","affiliation":[{"name":"Molecular Biology Division, Biomedical Research Foundation of the Academy of Athens, 115 27 Athens, Greece"},{"name":"Center for New Biotechnologies and Precision Medicine, Medical School, National and Kapodistrian University of Athens, 115 27 Athens, Greece"},{"name":"Clinical Genomics and Pharmacogenomics Unit, 4th Department of Internal Medicine, Medical School, National and Kapodistrian University of Athens, 115 27 Athens, Greece"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2020,12,16]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1161\/01.RES.0000107198.90218.21","article-title":"Phosphoproteome Analysis of Cardiomyocytes Subjected to \u03b2-Adrenergic Stimulation: Identification and characterization of a cardiac heat shock protein p20","volume":"94","author":"Chu","year":"2004","journal-title":"Circ. Res."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"15302","DOI":"10.1016\/S0021-9258(17)36606-1","article-title":"Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin","volume":"269","author":"Kato","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"3154","DOI":"10.1002\/pmic.200401356","article-title":"Changes in the rat heart proteome induced by exercise training: Increased abundance of heat shock protein hsp20","volume":"6","author":"Boluyt","year":"2006","journal-title":"Proteomics"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.cardfail.2005.07.006","article-title":"Proteomic Analysis Reveals Significant Alternations of Cardiac Small Heat Shock Protein Expression in Congestive Heart Failure","volume":"12","author":"Dohke","year":"2006","journal-title":"J. Card. Fail."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1474","DOI":"10.1161\/01.RES.0000129179.66631.00","article-title":"Small Heat-Shock Protein Hsp20 Phosphorylation Inhibits \u03b2-Agonist-Induced Cardiac Apoptosis","volume":"94","author":"Fan","year":"2004","journal-title":"Circ. Res."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1161\/CIRCRESAHA.109.200378","article-title":"Blockade of Hsp20 phosphorylation exacerbates cardiac ischemia\/reperfusion injury by suppressed autophagy and increased cell death","volume":"105","author":"Qian","year":"2009","journal-title":"Circ. Res."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1792","DOI":"10.1161\/01.CIR.0000160851.41872.C6","article-title":"Novel Cardioprotective Role of a Small Heat-Shock Protein, Hsp20, Against Ischemia\/Reperfusion Injury","volume":"111","author":"Fan","year":"2005","journal-title":"Circulation"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1161\/01.RES.0000251074.19348.af","article-title":"Small Heat-Shock Protein Hsp20 Attenuates \u03b2-Agonist\u2014Mediated Cardiac Remodeling Through Apoptosis Signal\u2014Regulating Kinase 1","volume":"99","author":"Fan","year":"2006","journal-title":"Circ. Res."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2357","DOI":"10.1161\/CIRCULATIONAHA.108.814145","article-title":"MicroRNA-320 Is Involved in the Regulation of Cardiac Ischemia\/Reperfusion Injury by Targeting Heat-Shock Protein 20","volume":"119","author":"Ren","year":"2009","journal-title":"Circulation"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1042\/BST20110673","article-title":"PKA phosphorylation of the small heat-shock protein Hsp20 enhances its cardioprotective effects","volume":"40","author":"Edwards","year":"2012","journal-title":"Biochem. Soc. Trans."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1016\/j.tcm.2005.05.004","article-title":"Hsp20 and Its Cardioprotection","volume":"15","author":"Fan","year":"2005","journal-title":"Trends Cardiovasc. Med."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1080\/15548627.2017.1392420","article-title":"Regulation of BECN1-mediated autophagy by HSPB6: Insights from a human HSPB6S10F mutant","volume":"14","author":"Liu","year":"2018","journal-title":"Autophagy"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"33465","DOI":"10.1074\/jbc.M802307200","article-title":"Human Mutation in the Anti-apoptotic Heat Shock Protein 20 Abrogates Its Cardioprotective Effects","volume":"283","author":"Nicolaou","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"3911","DOI":"10.1111\/jcmm.13665","article-title":"A novel human S10F-Hsp20 mutation induces lethal peripartum cardiomyopathy","volume":"22","author":"Liu","year":"2018","journal-title":"J. Cell. Mol. Med."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1270","DOI":"10.1161\/CIRCRESAHA.108.182832","article-title":"Heat Shock Protein 20 Interacting with Phosphorylated Akt Reduces Doxorubicin-Triggered Oxidative Stress and Cardiotoxicity","volume":"103","author":"Fan","year":"2008","journal-title":"Circ. Res."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1429","DOI":"10.1161\/CIRCRESAHA.110.237644","article-title":"Small Heat Shock Protein 20 Interacts with Protein Phosphatase-1 and Enhances Sarcoplasmic Reticulum Calcium Cycling","volume":"108","author":"Qian","year":"2011","journal-title":"Circ. Res."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1002\/cbf.3147","article-title":"Heat shock protein 20 (HSP20) is a novel substrate for protein kinase D1 (PKD1)","volume":"33","author":"Sin","year":"2015","journal-title":"Cell Biochem. Funct."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1016\/j.yjmcc.2011.02.006","article-title":"Disruption of the cyclic AMP phosphodiesterase-4 (PDE4)\u2013HSP20 complex attenuates the \u03b2-agonist induced hypertrophic response in cardiac myocytes","volume":"50","author":"Sin","year":"2011","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"2394","DOI":"10.1074\/jbc.M311324200","article-title":"Interaction of Human HSP22 (HSPB8) with Other Small Heat Shock Proteins","volume":"279","author":"Sun","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1007\/s11010-006-9266-8","article-title":"Small heat shock protein Hsp20 (HspB6) as a partner of 14-3-3\u03b3","volume":"295","author":"Chernik","year":"2007","journal-title":"Mol. Cell. Biochem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1096\/fj.04-2911fje","article-title":"Transducible heat shock protein 20 (HSP20) phosphopeptide alters cytoskeletal dynamics","volume":"19","author":"Dreiza","year":"2004","journal-title":"FASEB J."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"6127","DOI":"10.1021\/bi300674e","article-title":"Monomeric 14-3-3\u03b6 Has a Chaperone-Like Activity and Is Stabilized by Phosphorylated HspB6","volume":"51","author":"Sluchanko","year":"2012","journal-title":"Biochemistry"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.abb.2012.03.010","article-title":"Cofilin weakly interacts with 14-3-3 and therefore can only indirectly participate in regulation of cell motility by small heat shock protein HspB6 (Hsp20)","volume":"521","author":"Sudnitsyna","year":"2012","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/S0022-4804(03)00113-6","article-title":"The small heat shock protein (HSP)20 is dynamically associated with the actin cross-linking protein actinin","volume":"111","author":"Tessier","year":"2003","journal-title":"J. Surg. Res."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1042\/BST20130272","article-title":"The cardioprotective role of small heat-shock protein 20","volume":"42","author":"Martin","year":"2014","journal-title":"Biochem. Soc. Trans."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"3211","DOI":"10.1242\/jcs.187849","article-title":"Cellular functions of the ADF\/cofilin family at a glance","volume":"129","author":"Kanellos","year":"2016","journal-title":"J. Cell Sci."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1161\/01.CIR.0000044386.27444.5A","article-title":"Localization, macromolecular associations, and function of the small heat shock-related protein HSP20 in rat heart","volume":"107","author":"Pipkin","year":"2003","journal-title":"Circulation"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1016\/S0171-9335(99)80022-3","article-title":"The small heat shock proteins Hsp20 and \u03b1B-crystallin in cultured cardiac myocytes: Differences in cellular localization and solubilization after heat stress","volume":"78","year":"1999","journal-title":"Eur. J. Cell Biol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.semcancer.2006.03.005","article-title":"14-3-3 proteins: A historic overview","volume":"16","author":"Aitken","year":"2006","journal-title":"Semin. Cancer Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1016\/S0092-8674(00)81067-3","article-title":"Interaction of 14-3-3 with Signaling Proteins Is Mediated by the Recognition of Phosphoserine","volume":"84","author":"Muslin","year":"1996","journal-title":"Cell"},{"key":"ref_31","first-page":"1528","article-title":"14-3-3 Proteins and regulation of cytoskeleton","volume":"75","author":"Sluchanko","year":"2010","journal-title":"Biochemistry"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1016\/S0092-8674(00)80487-0","article-title":"The Structural Basis for 14-3-3: Phosphopeptide Binding Specificity","volume":"91","author":"Yaffe","year":"1997","journal-title":"Cell"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/bs.pmbts.2019.03.007","article-title":"Intrinsic disorder associated with 14-3-3 proteins and their partners","volume":"166","author":"Sluchanko","year":"2019","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"bat085","DOI":"10.1093\/database\/bat085","article-title":"ANIA: ANnotation and Integrated Analysis of the 14-3-3 interactome","volume":"2014","author":"Tinti","year":"2014","journal-title":"Database"},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Ballone, A., Centorrino, F., and Ottmann, C. (2018). 14-3-3: A Case Study in PPI Modulation. Molecules, 23.","DOI":"10.3390\/molecules23061386"},{"key":"ref_36","first-page":"11","article-title":"14-3-3 proteins: A family of versatile molecular regulators","volume":"57","author":"Silhan","year":"2008","journal-title":"Physiol. Res."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"re10","DOI":"10.1126\/stke.2962005re10","article-title":"14-3-3 Proteins: A Number of Functions for a Numbered Protein","volume":"2005","author":"Bridges","year":"2005","journal-title":"Sci. STKE"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1089\/ten.tea.2018.0169","article-title":"Nanotechnology Enabled Modulation of Signaling Pathways Affects Physiologic Responses in Intact Vascular Tissue","volume":"25","author":"Hocking","year":"2019","journal-title":"Tissue Eng. Part A"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1007\/s00418-004-0711-z","article-title":"Comparison of the small heat shock proteins \u03b1B-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle","volume":"122","author":"Golenhofen","year":"2000","journal-title":"Histochem. Cell Biol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/j.carpath.2005.03.006","article-title":"Myocardial ischemia and reperfusion injury","volume":"14","author":"Buja","year":"2005","journal-title":"Cardiovasc. Pathol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.bcp.2008.03.016","article-title":"Cytoskeleton and apoptosis","volume":"76","author":"Hamelin","year":"2008","journal-title":"Biochem. Pharmacol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1042\/BJ20080320","article-title":"A role for actin in regulating apoptosis\/programmed cell death: Evidence spanning yeast, plants and animals","volume":"413","author":"Gourlay","year":"2008","journal-title":"Biochem. J."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/nrm1682","article-title":"The actin cytoskeleton: A key regulator of apoptosis and ageing?","volume":"6","author":"Gourlay","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.phrs.2014.08.004","article-title":"Novel therapeutic strategies for ischemic heart disease","volume":"89","author":"Perricone","year":"2014","journal-title":"Pharmacol. Res."},{"key":"ref_45","first-page":"G339","article-title":"Ischemia-mediated aggregation of the actin cytoskeleton is one of the major initial events resulting in ischemia-reperfusion injury","volume":"296","author":"Shi","year":"2009","journal-title":"Am. J. Physiol. Liver Physiol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1537","DOI":"10.1016\/j.jmb.2015.02.002","article-title":"A First Line of Stress Defense: Small Heat Shock Proteins and Their Function in Protein Homeostasis","volume":"427","author":"Haslbeck","year":"2015","journal-title":"J. Mol. Biol."},{"key":"ref_47","first-page":"511","article-title":"Structure and Properties of Small Heat Shock Proteins (sHsp) and Their Interaction with Cytoskeleton Proteins","volume":"67","author":"Gusev","year":"2002","journal-title":"Biochemistry"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1379\/1466-1268(2002)007<0167:ACASHS>2.0.CO;2","article-title":"Actin cytoskeleton and small heat shock proteins: How do they interact?","volume":"7","author":"Mounier","year":"2002","journal-title":"Cell Stress Chaperon"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1165\/rcmb.2007-0263OC","article-title":"Cyclic Strain\u2013Induced HSP27 Phosphorylation Modulates Actin Filaments in Airway Smooth Muscle Cells","volume":"39","author":"Chaudhuri","year":"2008","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1212","DOI":"10.1161\/ATVBAHA.109.198440","article-title":"Low-Density Lipoproteins Induce Heat Shock Protein 27 Dephosphorylation, Oligomerization, and Subcellular Relocalization in Human Vascular Smooth Muscle Cells","volume":"30","author":"Padro","year":"2010","journal-title":"Arter. Thromb. Vasc. Biol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1016\/j.yjmcc.2010.06.004","article-title":"Protective effect of phosphorylated Hsp27 in coronary arteries through actin stabilization","volume":"49","author":"Robinson","year":"2010","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.yexcr.2015.08.002","article-title":"Expression of heat shock protein 27 correlates with actin cytoskeletal dynamics and contractility of cultured human bladder smooth muscle cells","volume":"338","author":"Wang","year":"2015","journal-title":"Exp. Cell Res."},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Vafiadaki, E., Arvanitis, D.A., Sanoudou, D., and Kranias, E.G. (2013). Identification of a Protein Phosphatase-1\/Phospholamban Complex That Is Regulated by cAMP-Dependent Phosphorylation. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0080867"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1086\/510402","article-title":"Nemaline Myopathy with Minicores Caused by Mutation of the CFL2 Gene Encoding the Skeletal Muscle Actin\u2014Binding Protein, Cofilin-2","volume":"80","author":"Agrawal","year":"2007","journal-title":"Am. J. Hum. Genet."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2341","DOI":"10.1093\/hmg\/dds053","article-title":"Normal myofibrillar development followed by progressive sarcomeric disruption with actin accumulations in a mouse Cfl2 knockout demonstrates requirement of cofilin-2 for muscle maintenance","volume":"21","author":"Agrawal","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1016\/j.ejcb.2014.01.007","article-title":"Severe protein aggregate myopathy in a knockout mouse model points to an essential role of cofilin2 in sarcomeric actin exchange and muscle maintenance","volume":"93","author":"Gurniak","year":"2014","journal-title":"Eur. J. Cell Biol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"6046","DOI":"10.1128\/MCB.00654-09","article-title":"Muscle Lim Protein Interacts with Cofilin 2 and Regulates F-Actin Dynamics in Cardiac and Skeletal Muscle","volume":"29","author":"Papalouka","year":"2009","journal-title":"Mol. Cell. Biol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.jmb.2006.10.057","article-title":"Phospholamban Interacts with HAX-1, a Mitochondrial Protein with Anti-apoptotic Function","volume":"367","author":"Vafiadaki","year":"2007","journal-title":"J. Mol. Biol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1091\/mbc.e08-06-0587","article-title":"The Anti-apoptotic Protein HAX-1 Interacts with SERCA2 and Regulates Its Protein Levels to Promote Cell Survival","volume":"20","author":"Vafiadaki","year":"2009","journal-title":"Mol. Biol. Cell"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"2308","DOI":"10.1016\/j.bbamcr.2017.08.010","article-title":"Muscle Lim Protein and myosin binding protein C form a complex regulating muscle differentiation","volume":"1864","author":"Arvanitis","year":"2017","journal-title":"Biochim. Biophys. Acta BBA Bioenerg."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"3261","DOI":"10.1111\/febs.12859","article-title":"Muscle lim protein isoform negatively regulates striated muscle actin dynamics and differentiation","volume":"281","author":"Vafiadaki","year":"2014","journal-title":"FEBS J."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1161\/CIRCRESAHA.112.279935","article-title":"Novel role of HAX-1 in ischemic injury protection involvement of heat shock protein 90","volume":"112","author":"Lam","year":"2013","journal-title":"Circ. Res."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1093\/cvr\/cvv127","article-title":"A novel human R25C-phospholamban mutation is associated with super-inhibition of calcium cycling and ventricular arrhythmia","volume":"107","author":"Liu","year":"2015","journal-title":"Cardiovasc. Res."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/24\/9572\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T10:45:40Z","timestamp":1760179540000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/24\/9572"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,12,16]]},"references-count":63,"journal-issue":{"issue":"24","published-online":{"date-parts":[[2020,12]]}},"alternative-id":["ijms21249572"],"URL":"https:\/\/doi.org\/10.3390\/ijms21249572","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,12,16]]}}}