{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T04:46:49Z","timestamp":1791607609641,"version":"4.3.4"},"reference-count":193,"publisher":"MDPI AG","issue":"18","license":[{"start":{"date-parts":[[2020,9,11]],"date-time":"2020-09-11T00:00:00Z","timestamp":1599782400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004923","name":"AFM-T\u00e9l\u00e9thon","doi-asserted-by":"publisher","award":["#19521"],"award-info":[{"award-number":["#19521"]}],"id":[{"id":"10.13039\/501100004923","id-type":"DOI","asserted-by":"publisher"}]},{"name":"IDEX-ISITE initiative (CAP 20e25)","award":["16-IDEX-0001"],"award-info":[{"award-number":["16-IDEX-0001"]}]},{"DOI":"10.13039\/501100002915","name":"Fondation pour la Recherche M\u00e9dicale","doi-asserted-by":"publisher","award":["DEQ20180339180"],"award-info":[{"award-number":["DEQ20180339180"]}],"id":[{"id":"10.13039\/501100002915","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010665","name":"H2020 Marie Sk\u0142odowska-Curie Actions","doi-asserted-by":"publisher","award":["GA 813599"],"award-info":[{"award-number":["GA 813599"]}],"id":[{"id":"10.13039\/100010665","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The E3 ubiquitin ligase MuRF1\/TRIM63 was identified 20 years ago and suspected to play important roles during skeletal muscle atrophy. Since then, numerous studies have been conducted to decipher the roles, molecular mechanisms and regulation of this enzyme. This revealed that MuRF1 is an important player in the skeletal muscle atrophy process occurring during catabolic states, making MuRF1 a prime candidate for pharmacological treatments against muscle wasting. Indeed, muscle wasting is an associated event of several diseases (e.g., cancer, sepsis, diabetes, renal failure, etc.) and negatively impacts the prognosis of patients, which has stimulated the search for MuRF1 inhibitory molecules. However, studies on MuRF1 cardiac functions revealed that MuRF1 is also cardioprotective, revealing a yin and yang role of MuRF1, being detrimental in skeletal muscle and beneficial in the heart. This review discusses data obtained on MuRF1, both in skeletal and cardiac muscles, over the past 20 years, regarding the structure, the regulation, the location and the different functions identified, and the first inhibitors reported, and aim to draw the picture of what is known about MuRF1. The review also discusses important MuRF1 characteristics to consider for the design of future drugs to maintain skeletal muscle mass in patients with different pathologies.<\/jats:p>","DOI":"10.3390\/ijms21186663","type":"journal-article","created":{"date-parts":[[2020,9,13]],"date-time":"2020-09-13T21:11:32Z","timestamp":1600031492000},"page":"6663","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":139,"title":["MuRF1\/TRIM63, Master Regulator of Muscle Mass"],"prefix":"10.3390","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6818-5900","authenticated-orcid":false,"given":"Dulce","family":"Peris-Moreno","sequence":"first","affiliation":[{"name":"INRA, UNH, Unit\u00e9 de Nutrition Humaine, Universit\u00e9 Clermont Auvergne, F-63000 Clermont-Ferrand, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Taillandier","sequence":"additional","affiliation":[{"name":"INRA, UNH, Unit\u00e9 de Nutrition Humaine, Universit\u00e9 Clermont Auvergne, F-63000 Clermont-Ferrand, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8730-5776","authenticated-orcid":false,"given":"C\u00e9cile","family":"Polge","sequence":"additional","affiliation":[{"name":"INRA, UNH, Unit\u00e9 de Nutrition Humaine, Universit\u00e9 Clermont Auvergne, F-63000 Clermont-Ferrand, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,9,11]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1146\/annurev-biochem-060815-014922","article-title":"Ubiquitin Ligases: Structure, Function, and Regulation","volume":"86","author":"Zheng","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1006\/jmbi.2001.4448","article-title":"Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain","volume":"306","author":"Centner","year":"2001","journal-title":"J. Mol. Biol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1704","DOI":"10.1126\/science.1065874","article-title":"Identification of ubiquitin ligases required for skeletal muscle atrophy","volume":"294","author":"Bodine","year":"2001","journal-title":"Science"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/j.biochi.2019.07.014","article-title":"Skeletal muscle atrogenes: From rodent models to human pathologies","volume":"166","author":"Taillandier","year":"2019","journal-title":"Biochimie"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1016\/0968-0004(92)90308-V","article-title":"A novel zinc finger coiled-coil domain in a family of nuclear proteins","volume":"17","author":"Reddy","year":"1992","journal-title":"Trends Biochem. Sci."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1002\/bies.20304","article-title":"TRIM\/RBCC, a novel class of \u2018single protein RING finger\u2019 E3 ubiquitin ligases","volume":"27","author":"Meroni","year":"2005","journal-title":"BioEssays"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"2140","DOI":"10.1093\/emboj\/20.9.2140","article-title":"The tripartite motif family identifies cell compartments","volume":"20","author":"Reymond","year":"2001","journal-title":"EMBO J."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"8970","DOI":"10.1074\/jbc.M512755200","article-title":"Subclassification of the RBCC\/TRIM superfamily reveals a novel motif necessary for microtubule binding","volume":"281","author":"Short","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Caratozzolo, M.F., Marzano, F., Mastropasqua, F., Sbis\u00e0, E., and Tullo, A. (2017). TRIM8: Making the Right Decision between the Oncogene and Tumour Suppressor Role. Genes, 8.","DOI":"10.3390\/genes8120354"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.tcm.2018.05.007","article-title":"A systematic view on E3 ligase Ring TRIMmers with a focus on cardiac function and disease","volume":"29","author":"Borlepawar","year":"2019","journal-title":"Trends Cardiovasc. Med."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Sardiello, M., Cairo, S., Fontanella, B., Ballabio, A., and Meroni, G. (2008). Genomic analysis of the TRIM family reveals two groups of genes with distinct evolutionary properties. BMC Evol. Biol., 8.","DOI":"10.1186\/1471-2148-8-225"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Carthagena, L., Bergamaschi, A., Luna, J.M., David, A., Uchil, P.D., Margottin-Goguet, F., Mothes, W., Hazan, U., Transy, C., and Pancino, G. (2009). Human TRIM Gene Expression in Response to Interferons. PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0004894"},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Mar\u00edn, I. (2012). Origin and Diversification of TRIM Ubiquitin Ligases. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0050030"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1038\/nri2413","article-title":"TRIM family proteins and their emerging roles in innate immunity","volume":"8","author":"Ozato","year":"2008","journal-title":"Nat. Rev. Immunol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1146\/annurev.biochem.78.101807.093809","article-title":"RING Domain E3 Ubiquitin Ligases","volume":"78","author":"Deshaies","year":"2009","journal-title":"Annu. Rev. Biochem."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1042\/BST20160325","article-title":"Structural determinants of TRIM protein function","volume":"45","author":"Esposito","year":"2017","journal-title":"Biochem. Soc. Trans."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"10722","DOI":"10.1021\/bi800733z","article-title":"Structural analysis of B-Box 2 from MuRF1: Identification of a novel self-association pattern in a RING-like fold","volume":"47","author":"Mrosek","year":"2008","journal-title":"Biochemistry"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/cddiscovery.2017.71","article-title":"Zinc-finger proteins in health and disease","volume":"3","author":"Cassandri","year":"2017","journal-title":"Cell Death Discov."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.tibs.2011.11.001","article-title":"RINGs hold the key to ubiquitin transfer","volume":"37","author":"Budhidarmo","year":"2012","journal-title":"Trends Biochem. Sci."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"762","DOI":"10.1038\/cr.2014.46","article-title":"Structural insights into the TRIM family of ubiquitin E3 ligases","volume":"24","author":"Li","year":"2014","journal-title":"Cell Res."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/j.jmb.2005.05.021","article-title":"MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: Towards understanding MURF-dependent muscle ubiquitination","volume":"350","author":"Witt","year":"2005","journal-title":"J. Mol. Biol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1016\/j.ajpath.2010.11.049","article-title":"The ubiquitin ligase MuRF1 protects against cardiac ischemia\/reperfusion injury by its proteasome-dependent degradation of phospho-c-Jun","volume":"178","author":"Li","year":"2011","journal-title":"Am. J. Pathol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"2900","DOI":"10.1016\/j.jmb.2019.05.025","article-title":"Exploration of the TRIM Fold of MuRF1 Using EPR Reveals a Canonical Antiparallel Structure and Extended COS-Box","volume":"431","author":"Stevens","year":"2019","journal-title":"J. Mol. Biol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1083\/jcb.150.4.771","article-title":"Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein","volume":"150","author":"Spencer","year":"2000","journal-title":"J. Cell Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"e16309","DOI":"10.7554\/eLife.16309","article-title":"Mechanism of B-box 2 domain-mediated higher-order assembly of the retroviral restriction factor TRIM5\u03b1","volume":"5","author":"Wagner","year":"2016","journal-title":"Elife"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1563","DOI":"10.1242\/jcs.110.14.1563","article-title":"Involvement of the rfp tripartite motif in protein-protein interactions and subcellular distribution","volume":"110 Pt 14","author":"Cao","year":"1997","journal-title":"J. Cell Sci."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Franke, B., Gasch, A., Rodriguez, D., Chami, M., Khan, M.M., Rudolf, R., Bibby, J., Hanashima, A., Bogomolovas, J., and von Castelmur, E. (2014). Molecular basis for the fold organization and sarcomeric targeting of the muscle atrogin MuRF1. Open Biol., 4.","DOI":"10.1098\/rsob.130172"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"18135","DOI":"10.1073\/pnas.0404341102","article-title":"Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I","volume":"101","author":"Kedar","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1224","DOI":"10.1016\/j.jmb.2007.11.049","article-title":"Muscle RING-finger protein-1 (MuRF1) as a connector of muscle energy metabolism and protein synthesis","volume":"376","author":"Koyama","year":"2008","journal-title":"J. Mol. Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1758","DOI":"10.1002\/pro.3690","article-title":"Structural basis of generic versus specific E2\u2013RING E3 interactions in protein ubiquitination","volume":"28","author":"Gundogdu","year":"2019","journal-title":"Protein Sci."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1038\/sj.emboj.7601952","article-title":"Cooperative control of striated muscle mass and metabolism by MuRF1 and MuRF2","volume":"27","author":"Witt","year":"2008","journal-title":"EMBO J."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1007\/s10974-012-9288-7","article-title":"Developmental regulation of MURF E3 ubiquitin ligases in skeletal muscle","volume":"33","author":"Perera","year":"2012","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"4469","DOI":"10.1242\/jcs.00131","article-title":"Transient association of titin and myosin with microtubules in nascent myofibrils directed by the MURF2 RING-finger protein","volume":"115","author":"Pizon","year":"2002","journal-title":"J. Cell Sci."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"2007","DOI":"10.1113\/jphysiol.2010.202044","article-title":"Preferential skeletal muscle myosin loss in response to mechanical silencing in a novel rat intensive care unit model: Underlying mechanisms","volume":"589","author":"Ochala","year":"2011","journal-title":"J. Physiol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1186\/s13395-020-00229-2","article-title":"Expression of MuRF1 or MuRF2 is essential for the induction of skeletal muscle atrophy and dysfunction in a murine pulmonary hypertension model","volume":"10","author":"Nguyen","year":"2020","journal-title":"Skelet. Muscle"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1096\/fj.03-0610com","article-title":"Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression","volume":"18","author":"Lecker","year":"2004","journal-title":"FASEB J."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1697","DOI":"10.1096\/fj.02-0312com","article-title":"Patterns of gene expression in atrophying skeletal muscles: Response to food deprivation","volume":"16","author":"Jagoe","year":"2002","journal-title":"FASEB J."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1016\/j.biocel.2016.06.019","article-title":"UBE2D2 is not involved in MuRF1-dependent muscle wasting during hindlimb suspension","volume":"79","author":"Polge","year":"2016","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"3727","DOI":"10.1113\/JP278073","article-title":"UBR5 is a novel E3 ubiquitin ligase involved in skeletal muscle hypertrophy and recovery from atrophy","volume":"597","author":"Seaborne","year":"2019","journal-title":"J. Physiol."},{"key":"ref_40","first-page":"108","article-title":"Electrical stimulation delays reinnervation in denervated rat muscle","volume":"56","author":"Erbereli","year":"2017","journal-title":"Muscle Nerve"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"5268","DOI":"10.1096\/fj.201700089RR","article-title":"Transcriptomic and epigenetic regulation of disuse atrophy and the return to activity in skeletal muscle","volume":"31","author":"Fisher","year":"2017","journal-title":"FASEB J."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"800","DOI":"10.1002\/mus.21578","article-title":"Leucine attenuates skeletal muscle wasting via inhibition of ubiquitin ligases","volume":"41","author":"Baptista","year":"2010","journal-title":"Muscle Nerve"},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Baptista, I.L., Silva, W.J., Artioli, G.G., Guilherme, J.P.L.F., Leal, M.L., Aoki, M.S., Miyabara, E.H., and Moriscot, A.S. (2013). Leucine and HMB differentially modulate proteasome system in skeletal muscle under different sarcopenic conditions. PLoS ONE, 8.","DOI":"10.1371\/annotation\/9060434b-c1df-4d52-8cda-88b9fbfaea51"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1007\/s00441-017-2614-z","article-title":"FoxO3a suppression and VPS34 activity are essential to anti-atrophic effects of leucine in skeletal muscle","volume":"369","author":"Baptista","year":"2017","journal-title":"Cell Tissue Res."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1152\/ajpendo.00073.2004","article-title":"IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1","volume":"287","author":"Sacheck","year":"2004","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"3900","DOI":"10.1210\/en.2008-0439","article-title":"Role of Akt\/GSK-3beta\/beta-catenin transduction pathway in the muscle anti-atrophy action of insulin-like growth factor-I in glucocorticoid-treated rats","volume":"149","author":"Schakman","year":"2008","journal-title":"Endocrinology"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"R1332","DOI":"10.1152\/ajpregu.00272.2009","article-title":"Insulin-like growth factor-I and genetic effects on indexes of protein degradation in response to feed deprivation in rainbow trout (Oncorhynchus mykiss)","volume":"297","author":"Cleveland","year":"2009","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"e14158","DOI":"10.14814\/phy2.14158","article-title":"Insulin and exercise improved muscle function in rats with severe burns and hindlimb unloading","volume":"7","author":"Song","year":"2019","journal-title":"Physiol. Rep."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"H1565","DOI":"10.1152\/ajpheart.00146.2010","article-title":"IGF-1 prevents ANG II-induced skeletal muscle atrophy via Akt- and Foxo-dependent inhibition of the ubiquitin ligase atrogin-1 expression","volume":"298","author":"Yoshida","year":"2010","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1152\/ajpendo.00060.2012","article-title":"Role of IGF-I and the TNF\u03b1\/NF-\u03baB pathway in the induction of muscle atrogenes by acute inflammation","volume":"303","author":"Schakman","year":"2012","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1038\/nrd4467","article-title":"Muscle wasting in disease: Molecular mechanisms and promising therapies","volume":"14","author":"Cohen","year":"2015","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1042\/bj20030022","article-title":"Forkhead transcription factor FOXO1 (FKHR)-dependent induction of PDK4 gene expression in skeletal muscle during energy deprivation","volume":"375","author":"Furuyama","year":"2003","journal-title":"Biochem. J."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"899","DOI":"10.2337\/diabetes.53.4.899","article-title":"Protein Kinase B-\u03b1 Inhibits Human Pyruvate Dehydrogenase Kinase-4 Gene Induction by Dexamethasone Through Inactivation of FOXO Transcription Factors","volume":"53","author":"Kwon","year":"2004","journal-title":"Diabetes"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1152\/ajpendo.00646.2007","article-title":"The glucocorticoid receptor and FOXO1 synergistically activate the skeletal muscle atrophy-associated MuRF1 gene","volume":"295","author":"Waddell","year":"2008","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1016\/j.biocel.2010.01.006","article-title":"Sepsis increases the expression and activity of the transcription factor Forkhead Box O 1 (FOXO1) in skeletal muscle by a glucocorticoid-dependent mechanism","volume":"42","author":"Smith","year":"2010","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"C548","DOI":"10.1152\/ajpcell.00502.2008","article-title":"FoxO1 induces apoptosis in skeletal myotubes in a DNA-binding-dependent manner","volume":"297","author":"McLoughlin","year":"2009","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1038\/ki.2012.84","article-title":"Transcription factor FoxO1, the dominant mediator of muscle wasting in chronic kidney disease, is inhibited by microRNA-486","volume":"82","author":"Xu","year":"2012","journal-title":"Kidney Int."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1946","DOI":"10.1210\/me.2013-1194","article-title":"Smad3 induces atrogin-1, inhibits mTOR and protein synthesis, and promotes muscle atrophy in vivo","volume":"27","author":"Goodman","year":"2013","journal-title":"Mol. Endocrinol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"C278","DOI":"10.1152\/ajpcell.00391.2013","article-title":"SMAD3 augments FoxO3-induced MuRF-1 promoter activity in a DNA-binding-dependent manner","volume":"307","author":"Bollinger","year":"2014","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1152\/ajpendo.00389.2016","article-title":"Forkhead box O3 plays a role in skeletal muscle atrophy through expression of E3 ubiquitin ligases MuRF-1 and atrogin-1 in Cushing\u2019s syndrome","volume":"312","author":"Kang","year":"2017","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"Milan, G., Romanello, V., Pescatore, F., Armani, A., Paik, J.-H., Frasson, L., Seydel, A., Zhao, J., Abraham, R., and Goldberg, A.L. (2015). Regulation of autophagy and the ubiquitin\u2013proteasome system by the FoxO transcriptional network during muscle atrophy. Nat. Commun., 6.","DOI":"10.1038\/ncomms7670"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"C986","DOI":"10.1152\/ajpcell.00041.2008","article-title":"TNF induction of atrogin-1\/MAFbx mRNA depends on Foxo4 expression but not AKT-Foxo1\/3 signaling","volume":"295","author":"Moylan","year":"2008","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"556","DOI":"10.2337\/db18-0416","article-title":"FoxO Transcription Factors Are Critical Regulators of Diabetes-Related Muscle Atrophy","volume":"68","author":"Bhardwaj","year":"2019","journal-title":"Diabetes"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1038\/nature01667","article-title":"Insulin-regulated hepatic gluconeogenesis through FOXO1\u2013PGC-1\u03b1 interaction","volume":"423","author":"Puigserver","year":"2003","journal-title":"Nature"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"16260","DOI":"10.1073\/pnas.0607795103","article-title":"PGC-1\u03b1 protects skeletal muscle from atrophy by suppressing FoxO3 action and atrophy-specific gene transcription","volume":"103","author":"Sandri","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1210","DOI":"10.1152\/ajpendo.00512.2011","article-title":"A cell-autonomous role for the glucocorticoid receptor in skeletal muscle atrophy induced by systemic glucocorticoid exposure","volume":"302","author":"Watson","year":"2012","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"C762","DOI":"10.1152\/ajpcell.00361.2013","article-title":"NF-\u03baB but not FoxO sites in the MuRF1 promoter are required for transcriptional activation in disuse muscle atrophy","volume":"306","author":"Wu","year":"2014","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1152\/ajpendo.00240.2015","article-title":"Heightened TWEAK-NF-\u03baB signaling and inflammation-associated fibrosis in paralyzed muscles of men with chronic spinal cord injury","volume":"310","author":"Bickel","year":"2016","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_69","doi-asserted-by":"crossref","unstructured":"Vainshtein, A., and Sandri, M. (2020). Signaling Pathways that Control Muscle Mass. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21134759"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1164\/rccm.201106-1150OC","article-title":"A critical role for muscle ring finger-1 in acute lung injury-associated skeletal muscle wasting","volume":"185","author":"Files","year":"2012","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1210\/me.2013-1179","article-title":"Myostatin augments muscle-specific ring finger protein-1 expression through an NF-kB independent mechanism in SMAD3 null muscle","volume":"28","author":"Sriram","year":"2014","journal-title":"Mol. Endocrinol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1038\/sj.cdd.4400619","article-title":"Structure and function in the p53 family","volume":"6","author":"Arrowsmith","year":"1999","journal-title":"Cell Death Differ."},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Benosman, S., Meng, X., Grabowiecki, Y.V., Palamiuc, L., Hritcu, L., Gross, I., Mellitzer, G., Taya, Y., Loeffler, J.-P., and Gaiddon, C. (2011). Complex regulation of p73 isoforms after alteration of the amyloid precursor polypeptide (APP) function and DNA damages in neurons. J. Biol. Chem.","DOI":"10.1074\/jbc.M111.261271"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"724","DOI":"10.1038\/nrc2730","article-title":"The expanding universe of p53 targets","volume":"9","author":"Menendez","year":"2009","journal-title":"Nat. Rev. Cancer"},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Von Grabowiecki, Y., Abreu, P., Blanchard, O., Palamiuc, L., Benosman, S., M\u00e9riaux, S., Devignot, V., Gross, I., Mellitzer, G., and de Aguilar, J.L.G. (2016). Transcriptional activator TAp63 is upregulated in muscular atrophy during ALS and induces the pro-atrophic ubiquitin ligase Trim63. Elife, 5.","DOI":"10.7554\/eLife.10528"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1126\/science.1174447","article-title":"A gene network regulating lysosomal biogenesis and function","volume":"325","author":"Sardiello","year":"2009","journal-title":"Science"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"3852","DOI":"10.1093\/hmg\/ddr306","article-title":"Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways","volume":"20","author":"Palmieri","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1161\/CIRCRESAHA.114.305393","article-title":"Angiotensin II Induces Skeletal Muscle Atrophy by Activating TFEB-Mediated MuRF1 Expression","volume":"117","author":"Bois","year":"2015","journal-title":"Circ. Res."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1038\/364501a0","article-title":"Muscle deficiency and neonatal death in mice with a targeted mutation in the myogenin gene","volume":"364","author":"Hasty","year":"1993","journal-title":"Nature"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1038\/364532a0","article-title":"Myogenin gene disruption results in perinatal lethality because of severe muscle defect","volume":"364","author":"Nabeshima","year":"1993","journal-title":"Nature"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.cell.2010.09.004","article-title":"Myogenin and class II HDACs control neurogenic muscle atrophy by inducing E3 ubiquitin ligases","volume":"143","author":"Moresi","year":"2010","journal-title":"Cell"},{"key":"ref_82","first-page":"10697","article-title":"Regulation of muscle atrophy-related genes by the opposing transcriptional activities of ZEB1\/CtBP and FOXO3","volume":"46","author":"Ninfali","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/j.tcb.2007.07.004","article-title":"The C\/EBP family of transcription factors: A paradigm for interaction between gene expression and proliferation control","volume":"17","author":"Nerlov","year":"2007","journal-title":"Trends Cell Biol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"1737","DOI":"10.1002\/jcb.23093","article-title":"C\/EBP\u03b2 regulates dexamethasone-induced muscle cell atrophy and expression of atrogin-1 and MuRF1","volume":"112","author":"Gonnella","year":"2011","journal-title":"J. Cell. Biochem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1002\/jcsm.12145","article-title":"Activin A induces skeletal muscle catabolism via p38\u03b2 mitogen-activated protein kinase","volume":"8","author":"Ding","year":"2017","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"11177","DOI":"10.1074\/jbc.M115.641514","article-title":"Inhibition of Stat3 Activation Suppresses Caspase-3 and the Ubiquitin-Proteasome System, Leading to Preservation of Muscle Mass in Cancer Cachexia","volume":"290","author":"Silva","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"H1206","DOI":"10.1152\/ajpheart.00319.2008","article-title":"Hypertrophic cardiomyopathy in high-fat diet-induced obesity: Role of suppression of forkhead transcription factor and atrophy gene transcription","volume":"295","author":"Fang","year":"2008","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Shimizu, H., Langenbacher, A.D., Huang, J., Wang, K., Otto, G., Geisler, R., Wang, Y., and Chen, J.-N. (2017). The Calcineurin-FoxO-MuRF1 signaling pathway regulates myofibril integrity in cardiomyocytes. Elife, 6.","DOI":"10.7554\/eLife.27955"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1161\/CIRCRESAHA.111.252742","article-title":"AMP-activated protein kinase regulates E3 ligases in rodent heart","volume":"109","author":"Baskin","year":"2011","journal-title":"Circ. Res."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"9183","DOI":"10.1074\/jbc.M114.625715","article-title":"High CO2 levels cause skeletal muscle atrophy via AMP-activated kinase (AMPK), FoxO3a protein, and muscle-specific Ring finger protein 1 (MuRF1)","volume":"290","author":"Jaitovich","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1074\/mcp.M116.066159","article-title":"A Proteomic Approach to Identify Alterations in the Small Ubiquitin-like Modifier (SUMO) Network during Controlled Mechanical Ventilation in Rat Diaphragm Muscle","volume":"16","author":"Namuduri","year":"2017","journal-title":"Mol. Cell. Proteom."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1093\/jmcb\/mjy036","article-title":"Muscle RING-finger protein-1 (MuRF1) functions and cellular localization are regulated by SUMO1 post-translational modification","volume":"11","author":"Heras","year":"2019","journal-title":"J. Mol. Cell Biol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"17375","DOI":"10.1074\/jbc.M609659200","article-title":"Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages","volume":"282","author":"Kim","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1002\/jcsm.12233","article-title":"Small-molecule inhibition of MuRF1 attenuates skeletal muscle atrophy and dysfunction in cardiac cachexia","volume":"8","author":"Bowen","year":"2017","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_95","first-page":"1948","article-title":"Post-translationally modified muscle-specific ubiquitin ligases as circulating biomarkers in experimental cancer cachexia","volume":"7","author":"Mota","year":"2017","journal-title":"Am. J. Cancer Res."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"R971","DOI":"10.1152\/ajpregu.00617.2006","article-title":"Atrophy-related ubiquitin ligases atrogin-1 and MuRF-1 are associated with uterine smooth muscle involution in the postpartum period","volume":"292","author":"Bdolah","year":"2007","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"4294","DOI":"10.1111\/febs.12253","article-title":"Mechanisms regulating skeletal muscle growth and atrophy","volume":"280","author":"Schiaffino","year":"2013","journal-title":"FEBS J."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1447","DOI":"10.1152\/physrev.00031.2010","article-title":"Fiber types in mammalian skeletal muscles","volume":"91","author":"Schiaffino","year":"2011","journal-title":"Physiol. Rev."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1016\/j.jsb.2010.02.001","article-title":"MuRF1 is a muscle fiber-type II associated factor and together with MuRF2 regulates type-II fiber trophicity and maintenance","volume":"170","author":"Moriscot","year":"2010","journal-title":"J. Struct. Biol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1002\/jcsm.12060","article-title":"UBE2B is implicated in myofibrillar protein loss in catabolic C2C12 myotubes: UBE2B and myofibrillar protein degradation","volume":"7","author":"Polge","year":"2016","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_101","doi-asserted-by":"crossref","unstructured":"Belova, S.P., Mochalova, E.P., Kostrominova, T.Y., Shenkman, B.S., and Nemirovskaya, T.L. (2020). P38\u03b1-MAPK Signaling Inhibition Attenuates Soleus Atrophy during Early Stages of Muscle Unloading. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21082756"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"2149","DOI":"10.1002\/jcb.23136","article-title":"Myogenin regulates denervation-dependent muscle atrophy in mouse soleus muscle","volume":"112","author":"Macpherson","year":"2011","journal-title":"J. Cell. Biochem."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1152\/ajpendo.00257.2016","article-title":"Control of skeletal muscle atrophy in response to disuse: Clinical\/preclinical contentions and fallacies of evidence","volume":"311","author":"Atherton","year":"2016","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1083\/jcb.200108089","article-title":"Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1","volume":"157","author":"McElhinny","year":"2002","journal-title":"J. Cell Biol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"907","DOI":"10.1161\/CIRCRESAHA.112.270207","article-title":"Human molecular genetic and functional studies identify TRIM63, encoding Muscle RING Finger Protein 1, as a novel gene for human hypertrophic cardiomyopathy","volume":"111","author":"Chen","year":"2012","journal-title":"Circ. Res."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1083\/jcb.200901052","article-title":"During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation","volume":"185","author":"Cohen","year":"2009","journal-title":"J. Cell Biol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1083\/jcb.200402033","article-title":"Muscle ring finger protein-1 inhibits PKC{epsilon} activation and prevents cardiomyocyte hypertrophy","volume":"167","author":"Arya","year":"2004","journal-title":"J. Cell Biol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1186\/s13395-018-0156-z","article-title":"The complexity of titin splicing pattern in human adult skeletal muscles","volume":"8","author":"Savarese","year":"2018","journal-title":"Skelet. Muscle"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"1599","DOI":"10.1126\/science.1110463","article-title":"The kinase domain of titin controls muscle gene expression and protein turnover","volume":"308","author":"Lange","year":"2005","journal-title":"Science"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"3638","DOI":"10.1093\/hmg\/ddv108","article-title":"New cardiac and skeletal protein aggregate myopathy associated with combined MuRF1 and MuRF3 mutations","volume":"24","author":"Oldfors","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1111\/acel.12150","article-title":"Maintenance of muscle mass and load-induced growth in Muscle RING Finger 1 null mice with age","volume":"13","author":"Hwee","year":"2014","journal-title":"Aging Cell"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"693741","DOI":"10.1155\/2010\/693741","article-title":"Modulation of muscle atrophy, fatigue and MLC phosphorylation by MuRF1 as indicated by hindlimb suspension studies on MuRF1-KO mice","volume":"2010","author":"Labeit","year":"2010","journal-title":"J. Biomed. Biotechnol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1038\/ng.2772","article-title":"BMP signaling controls muscle mass","volume":"45","author":"Sartori","year":"2013","journal-title":"Nat. Genet."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1248","DOI":"10.1128\/MCB.06351-11","article-title":"The E3 ubiquitin ligase TRAF6 intercedes in starvation-induced skeletal muscle atrophy through multiple mechanisms","volume":"32","author":"Paul","year":"2012","journal-title":"Mol. Cell. Biol."},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Nagpal, P., Plant, P.J., Correa, J., Bain, A., Takeda, M., Kawabe, H., Rotin, D., Bain, J.R., and Batt, J.A.E. (2012). The ubiquitin ligase Nedd4-1 participates in denervation-induced skeletal muscle atrophy in mice. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0046427"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1186\/2044-5040-3-11","article-title":"Trip12, a HECT domain E3 ubiquitin ligase, targets Sox6 for proteasomal degradation and affects fiber type-specific gene expression in muscle cells","volume":"3","author":"An","year":"2013","journal-title":"Skelet. Muscle"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1016\/j.cmet.2007.09.009","article-title":"The E3 Ligase MuRF1 Degrades Myosin Heavy Chain Protein in Dexamethasone-Treated Skeletal Muscle","volume":"6","author":"Clarke","year":"2007","journal-title":"Cell Metab."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"4759","DOI":"10.1113\/jphysiol.2011.212845","article-title":"Muscle sparing in muscle RING finger 1 null mice: Response to synthetic glucocorticoids","volume":"589","author":"Baehr","year":"2011","journal-title":"J. Physiol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/0303-7207(77)90082-X","article-title":"The effect of cortisone on protein breakdown and synthesis in rat skeletal muscle","volume":"6","author":"Shoji","year":"1977","journal-title":"Mol. Cell. Endocrinol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1161\/CIRCHEARTFAILURE.113.000713","article-title":"Muscle-specific RING finger 1 negatively regulates pathological cardiac hypertrophy through downregulation of calcineurin A","volume":"7","author":"Maejima","year":"2014","journal-title":"Circ. Heart Fail."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1161\/01.RES.0000259559.48597.32","article-title":"Muscle ring finger 1, but not muscle ring finger 2, regulates cardiac hypertrophy in vivo","volume":"100","author":"Willis","year":"2007","journal-title":"Circ. Res."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1161\/CIRCRESAHA.109.194928","article-title":"Cardiac muscle ring finger-1 increases susceptibility to heart failure in vivo","volume":"105","author":"Willis","year":"2009","journal-title":"Circ. Res."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"e005234","DOI":"10.1161\/CIRCHEARTFAILURE.118.005234","article-title":"Doxorubicin Exposure Causes Subacute Cardiac Atrophy Dependent on the Striated Muscle-Specific Ubiquitin Ligase MuRF1","volume":"12","author":"Willis","year":"2019","journal-title":"Circ. Heart Fail."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1016\/S0895-7061(03)01018-5","article-title":"Changes in cardiovascular risk by reduction of left ventricular mass in hypertension: A meta-analysis","volume":"16","author":"Verdecchia","year":"2003","journal-title":"Am. J. Hypertens."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1007\/s00395-009-0068-5","article-title":"Depressed expression of MuRF1 and MAFbx in areas remote of recent myocardial infarction: A mechanism contributing to myocardial remodeling?","volume":"105","author":"Conraads","year":"2010","journal-title":"Basic Res. Cardiol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"143","DOI":"10.3233\/JND-180350","article-title":"Homozygous Nonsense Mutation p.Q274X in TRIM63 (MuRF1) in a Patient with Mild Skeletal Myopathy and Cardiac Hypertrophy","volume":"6","author":"Jokela","year":"2019","journal-title":"J. Neuromuscul. Dis."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1016\/j.jmb.2008.03.049","article-title":"MuRF1-dependent regulation of systemic carbohydrate metabolism as revealed from transgenic mouse studies","volume":"379","author":"Hirner","year":"2008","journal-title":"J. Mol. Biol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1271","DOI":"10.1007\/s00726-011-0877-3","article-title":"The creatine kinase system and pleiotropic effects of creatine","volume":"40","author":"Wallimann","year":"2011","journal-title":"Amino Acids"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"2486","DOI":"10.1172\/JCI32827","article-title":"Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3","volume":"117","author":"Fielitz","year":"2007","journal-title":"J. Clin. Investig."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1007\/s004410051315","article-title":"Sarcomeric myosin heavy chain is degraded by the proteasome","volume":"296","author":"Eble","year":"1999","journal-title":"Cell Tissue Res."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1096\/fj.00-0629fje","article-title":"Space shuttle flight (STS-90) enhances degradation of rat myosin heavy chain in association with activation of ubiquitin-proteasome pathway","volume":"15","author":"Ikemoto","year":"2001","journal-title":"FASEB J."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1093\/cvr\/cvp348","article-title":"Atrogin-1 and MuRF1 regulate cardiac MyBP-C levels via different mechanisms","volume":"85","author":"Mearini","year":"2010","journal-title":"Cardiovasc. Res."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"R1722","DOI":"10.1152\/ajpregu.00292.2007","article-title":"Contractile and connective tissue protein content of human skeletal muscle: Effects of 35 and 90 days of simulated microgravity and exercise countermeasures, American Journal of Physiology-Regulatory","volume":"293","author":"Haus","year":"2007","journal-title":"Integr. Comp. Physiol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1111\/j.1600-0838.2009.01029.x","article-title":"Myosin and actin content of human skeletal muscle fibers following 35 days bed rest","volume":"20","author":"Borina","year":"2010","journal-title":"Scand. J. Med. Sci. Sports"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"2722","DOI":"10.1002\/ijc.26298","article-title":"Myosin heavy chain is not selectively decreased in murine cancer cachexia","volume":"130","author":"Cosper","year":"2012","journal-title":"Int. J. Cancer"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"3790","DOI":"10.1096\/fj.11-180968","article-title":"Muscle actin is polyubiquitinylated in vitro and in vivo and targeted for breakdown by the E3 ligase MuRF1","volume":"25","author":"Polge","year":"2011","journal-title":"FASEB J."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"5302","DOI":"10.1074\/jbc.M610005200","article-title":"A new method of purification of proteasome substrates reveals polyubiquitination of 20 S proteasome subunits","volume":"282","author":"Ventadour","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1002\/jcsm.12249","article-title":"A muscle-specific MuRF1-E2 network requires stabilization of MuRF1-E2 complexes by telethonin, a newly identified substrate","volume":"9","author":"Polge","year":"2018","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/S0925-4439(02)00113-8","article-title":"Telethonin protein expression in neuromuscular disorders","volume":"1588","author":"Vainzof","year":"2002","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.ymgme.2005.10.008","article-title":"Genotype\u2014phenotype relationships involving hypertrophic cardiomyopathy-associated mutations in titin, muscle LIM protein, and telethonin","volume":"88","author":"Bos","year":"2006","journal-title":"Mol. Genet. Metab."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1016\/j.nmd.2016.07.003","article-title":"Novel mutation in TCAP manifesting with asymmetric calves and early-onset joint retractions","volume":"26","year":"2016","journal-title":"Neuromuscul. Disord."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1161\/CIRCRESAHA.111.245787","article-title":"Telethonin deficiency is associated with maladaptation to biomechanical stress in the mammalian heart","volume":"109","author":"Linke","year":"2011","journal-title":"Circ. Res."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1016\/S0092-8674(02)01226-6","article-title":"The Cardiac Mechanical Stretch Sensor Machinery Involves a Z Disc Complex that Is Defective in a Subset of Human Dilated Cardiomyopathy","volume":"111","author":"Hoshijima","year":"2002","journal-title":"Cell"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1002\/jcp.10158","article-title":"Titin-cap associates with, and regulates secretion of, Myostatin","volume":"193","author":"Nicholas","year":"2002","journal-title":"J. Cell. Physiol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1016\/j.jmb.2004.03.071","article-title":"The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle","volume":"339","author":"Kojic","year":"2004","journal-title":"J. Mol. Biol."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"13998","DOI":"10.1074\/jbc.M200712200","article-title":"Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins","volume":"277","author":"Frey","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"2544","DOI":"10.1016\/j.biocel.2008.04.013","article-title":"Coordinate expression of the 19S regulatory complex and evidence for ubiquitin-dependent telethonin degradation in the unloaded soleus muscle","volume":"40","author":"Heng","year":"2008","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"5238","DOI":"10.1016\/S0021-9258(17)42981-4","article-title":"Function of M-line-bound creatine kinase as intramyofibrillar ATP regenerator at the receiving end of the phosphorylcreatine shuttle in muscle","volume":"259","author":"Wallimann","year":"1984","journal-title":"J. Biol. Chem."},{"key":"ref_149","first-page":"125","article-title":"Myofibrillar creatine kinase and cardiac contraction","volume":"133","author":"Veksler","year":"1994","journal-title":"Mol. Cell. Biochem."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"1174","DOI":"10.1016\/j.cell.2010.12.001","article-title":"A Tissue-Specific Atlas of Mouse Protein Phosphorylation and Expression","volume":"143","author":"Huttlin","year":"2010","journal-title":"Cell"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1007\/s00018-008-8575-3","article-title":"Regulation of muscle creatine kinase by phosphorylation in normal and diabetic hearts","volume":"66","author":"Lin","year":"2009","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/j.cbpb.2009.01.012","article-title":"Creatine kinase regulation by reversible phosphorylation in frog muscle","volume":"152","author":"Dieni","year":"2009","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"12022","DOI":"10.1074\/jbc.M610363200","article-title":"The generation of the oxidized form of creatine kinase is a negative regulation on muscle creatine kinase","volume":"282","author":"Zhao","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.neulet.2008.04.023","article-title":"GMEB1, a novel endogenous caspase inhibitor, prevents hypoxia- and oxidative stress-induced neuronal apoptosis","volume":"438","author":"Nakagawa","year":"2008","journal-title":"Neurosci. Lett."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1007\/s10545-010-9236-x","article-title":"Enzymology of the branched-chain amino acid oxidation disorders: The valine pathway","volume":"35","author":"Wanders","year":"2012","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"6649","DOI":"10.1128\/MCB.25.15.6649-6659.2005","article-title":"Regulation of calcineurin through transcriptional induction of the calcineurin a beta promoter in vitro and in vivo","volume":"25","author":"Oka","year":"2005","journal-title":"Mol. Cell. Biol."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"3328","DOI":"10.1073\/pnas.041614798","article-title":"Myocyte-enriched calcineurin-interacting protein, MCIP1, inhibits cardiac hypertrophy in vivo","volume":"98","author":"Rothermel","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1038\/nm.2181","article-title":"CIB1 is a regulator of pathological cardiac hypertrophy","volume":"16","author":"Heineke","year":"2010","journal-title":"Nat. Med."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1038\/nrm1983","article-title":"Regulation of cardiac hypertrophy by intracellular signalling pathways","volume":"7","author":"Heineke","year":"2006","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/j.cardiores.2004.01.021","article-title":"Calcineurin\u2013NFAT signaling regulates the cardiac hypertrophic response in coordination with the MAPKs","volume":"63","author":"Molkentin","year":"2004","journal-title":"Cardiovasc. Res."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1038\/sj.bjp.0705873","article-title":"Inhibition of c-Jun N-terminal kinase decreases cardiomyocyte apoptosis and infarct size after myocardial ischemia and reperfusion in anaesthetized rats","volume":"142","author":"Ferrandi","year":"2004","journal-title":"Br. J. Pharmacol."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"H1828","DOI":"10.1152\/ajpheart.01117.2006","article-title":"A peptide inhibitor of c-Jun NH2-terminal kinase reduces myocardial ischemia-reperfusion injury and infarct size in vivo","volume":"292","author":"Milano","year":"2007","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1038\/nrm3495","article-title":"Molecular basis of physiological heart growth: Fundamental concepts and new players","volume":"14","author":"Maillet","year":"2013","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1152\/ajpendo.00326.2013","article-title":"Muscle RING finger-1 attenuates IGF-I-dependent cardiomyocyte hypertrophy by inhibiting JNK signaling","volume":"306","author":"Wadosky","year":"2014","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1152\/physiolgenomics.00040.2004","article-title":"Microarray analysis of gene expression after transverse aortic constriction in mice","volume":"19","author":"Zhao","year":"2004","journal-title":"Physiol. Genom."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"1663","DOI":"10.1007\/s11357-012-9468-9","article-title":"Regulation of nicotinic acetylcholine receptor turnover by MuRF1 connects muscle activity to endo\/lysosomal and atrophy pathways","volume":"35","author":"Rudolf","year":"2013","journal-title":"Age"},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1007\/s12013-010-9137-5","article-title":"The structure and function of endophilin proteins","volume":"60","author":"Kjaerulff","year":"2011","journal-title":"Cell Biochem. Biophys."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1016\/j.bpj.2016.06.017","article-title":"Association of Endophilin B1 with Cytoplasmic Vesicles","volume":"111","author":"Li","year":"2016","journal-title":"Biophys. J."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"1142","DOI":"10.1038\/ncb1634","article-title":"Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis","volume":"9","author":"Takahashi","year":"2007","journal-title":"Nat. Cell Biol."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"123","DOI":"10.4161\/auto.26841","article-title":"Role of autophagy, SQSTM1, SH3GLB1, and TRIM63 in the turnover of nicotinic acetylcholine receptors","volume":"10","author":"Khan","year":"2014","journal-title":"Autophagy"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1016\/j.celrep.2017.01.039","article-title":"CRL4DCAF8 Ubiquitin Ligase Targets Histone H3K79 and Promotes H3K9 Methylation in the Liver","volume":"18","author":"Li","year":"2017","journal-title":"Cell Rep."},{"key":"ref_172","doi-asserted-by":"crossref","unstructured":"Nowak, M., Suenkel, B., Porras, P., Migotti, R., Schmidt, F., Kny, M., Zhu, X., Wanker, E.E., Dittmar, G., and Fielitz, J. (2019). DCAF8, a novel MuRF1 interaction partner, promotes muscle atrophy. J. Cell Sci., 132.","DOI":"10.1242\/jcs.233395"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"17685","DOI":"10.1074\/jbc.M701429200","article-title":"Peroxisomal proliferator-activated receptor-alpha-dependent inhibition of endothelial cell proliferation and tumorigenesis","volume":"282","author":"Pozzi","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.mce.2015.06.008","article-title":"The ubiquitin ligase MuRF1 regulates PPAR\u03b1 activity in the heart by enhancing nuclear export via monoubiquitination","volume":"413","author":"Liao","year":"2015","journal-title":"Mol. Cell. Endocrinol."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1016\/j.cellsig.2017.03.005","article-title":"Long, Roles for RACK1 in cancer cell migration and invasion","volume":"35","author":"Duff","year":"2017","journal-title":"Cell. Signal"},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.1161\/01.RES.86.11.1173","article-title":"Cardiotrophic effects of protein kinase C epsilon: Analysis by in vivo modulation of PKCepsilon translocation","volume":"86","author":"Wu","year":"2000","journal-title":"Circ. Res."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1126\/science.7716516","article-title":"Localization of protein kinases by anchoring proteins: A theme in signal transduction","volume":"268","year":"1995","journal-title":"Science"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/S0955-0674(99)80003-9","article-title":"Muscle assembly: A titanic achievement?","volume":"11","author":"Gregorio","year":"1999","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1083\/jcb.151.3.639","article-title":"D-Titin: A giant protein with dual roles in chromosomes and muscles","volume":"151","author":"Machado","year":"2000","journal-title":"J. Cell Biol."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1093\/emboj\/16.2.211","article-title":"Molecular structure of the sarcomeric M band: Mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin","volume":"16","author":"Obermann","year":"1997","journal-title":"EMBO J."},{"key":"ref_181","doi-asserted-by":"crossref","unstructured":"Higashikuse, Y., Mittal, N., Arimura, T., Yoon, S.H., Oda, M., Enomoto, H., Kaneda, R., Hattori, F., Suzuki, T., and Kawakami, A. (2019). Perturbation of the titin\/MURF1 signaling complex is associated with hypertrophic cardiomyopathy in a fish model and in human patients. Dis. Models Mech., 12.","DOI":"10.1101\/680579"},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"2763","DOI":"10.3390\/ijms10062763","article-title":"Yeast Two-Hybrid, a Powerful Tool for Systems Biology","volume":"10","author":"Polge","year":"2009","journal-title":"Int. J. Mol. Sci."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1038\/cr.2016.35","article-title":"E2 enzymes: More than just middle men","volume":"26","author":"Stewart","year":"2016","journal-title":"Cell Res."},{"key":"ref_184","doi-asserted-by":"crossref","unstructured":"C\u00e9cile, P., Julien, A., Andrea, A., Agn\u00e8s, C., C\u00e9cile, C.-G., Clara, T., Christiane, D., Lydie, C., Daniel, B., and Marco, S. (2018). UBE2E1 Is Preferentially Expressed in the Cytoplasm of Slow-Twitch Fibers and Protects Skeletal Muscles from Exacerbated Atrophy upon Dexamethasone Treatment. Cells, 7.","DOI":"10.3390\/cells7110214"},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1007\/s12013-013-9627-3","article-title":"Comprehensive ubiquitin E2 profiling of ten ubiquitin E3 ligases","volume":"67","author":"Marblestone","year":"2013","journal-title":"Cell Biochem. Biophys."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1038\/msb.2009.55","article-title":"A comprehensive framework of E2-RING E3 interactions of the human ubiquitin-proteasome system","volume":"5","author":"Kemmeren","year":"2009","journal-title":"Mol. Syst. Biol."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"1905","DOI":"10.1101\/gr.093963.109","article-title":"Analysis of the human E2 ubiquitin conjugating enzyme protein interaction network","volume":"19","author":"Markson","year":"2009","journal-title":"Genome Res."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1042\/BJ20101487","article-title":"Functional interactions between ubiquitin E2 enzymes and TRIM proteins","volume":"434","author":"Napolitano","year":"2011","journal-title":"Biochem. J."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1007\/s11306-014-0695-1","article-title":"Non-targeted metabolomics analysis of cardiac Muscle Ring Finger-1 (MuRF1), MuRF2, and MuRF3 in vivo reveals novel and redundant metabolic changes","volume":"11","author":"Banerjee","year":"2015","journal-title":"Metabolomics"},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1042\/bse0410173","article-title":"The ubiquitin-proteasome system and skeletal muscle wasting","volume":"41","author":"Attaix","year":"2005","journal-title":"Essays Biochem."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1097\/00075197-200105000-00003","article-title":"What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?","volume":"4","author":"Jagoe","year":"2001","journal-title":"Curr. Opin. Clin. Nutr. Metab. Care"},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1007\/s12013-011-9175-7","article-title":"Targeting the ubiquitin E3 ligase MuRF1 to inhibit muscle atrophy","volume":"60","author":"Eddins","year":"2011","journal-title":"Cell Biochem. Biophys."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1002\/jcsm.12448","article-title":"Small-molecule-mediated chemical knock-down of MuRF1\/MuRF2 and attenuation of diaphragm dysfunction in chronic heart failure","volume":"10","author":"Adams","year":"2019","journal-title":"J. Cachexia Sarcopenia Muscle"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/18\/6663\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T10:09:16Z","timestamp":1760177356000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/18\/6663"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,9,11]]},"references-count":193,"journal-issue":{"issue":"18","published-online":{"date-parts":[[2020,9]]}},"alternative-id":["ijms21186663"],"URL":"https:\/\/doi.org\/10.3390\/ijms21186663","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,9,11]]}}}