{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,7,30]],"date-time":"2025-07-30T14:03:21Z","timestamp":1753884201767,"version":"3.41.2"},"reference-count":27,"publisher":"The Company of Biologists","issue":"9","license":[{"start":{"date-parts":[[2024,9,25]],"date-time":"2024-09-25T00:00:00Z","timestamp":1727222400000},"content-version":"vor","delay-in-days":10,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["SCBioCRAFT Cobre","P20GM121342 SC TRIMH Cobre"],"award-info":[{"award-number":["SCBioCRAFT Cobre","P20GM121342 SC TRIMH Cobre"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100006498","name":"Clemson University","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100006498","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,9,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n               <jats:p>TGF\u03b2-activated kinase-1 (TAK1) is phosphorylated during both muscle growth and muscle wasting. To understand how this can lead to such opposite effects, we first performed multiplex kinase array of mouse embryonic stem cells with and without stimulation of TAK1 to determine its potential downstream targets. The phosphorylation of these targets was then compared in three different models: hypertrophic longissimus muscle of Texel sheep, tibialis anterior muscle of mice with cancer-induced cachexia and C2C12-derived myofibers, with and without blockade of TAK1 phosphorylation. In both Texel sheep and in cancer-induced cachexia, phosphorylation of both TAK1 and p38 was increased. Whereas p90RSK was increased in Texel sheep but not cachexia and the phosphorylation of HSP27 and total Jnk were increased in cachexia but not Texel. To understand this further, we examined the expression of these proteins in C2C12 cells as they differentiated into myotubes, with and without blockade of TAK1 phosphorylation. In C2C12 cells, decreased phosphorylation of TAK1 leads to reduced phosphorylation of p38, JNK, and HSP27 after 16\u2005h and muscle fiber hypertrophy after 3 days. However, continuous blockade of this pathway leads to muscle fiber failure, suggesting that the timing of TAK1 activation controls the expression of context-dependent targets.<\/jats:p>","DOI":"10.1242\/bio.060487","type":"journal-article","created":{"date-parts":[[2024,8,30]],"date-time":"2024-08-30T08:41:22Z","timestamp":1725007282000},"source":"Crossref","is-referenced-by-count":0,"title":["Analysis of potential TAK1\/Map3k7 phosphorylation targets in hypertrophy and cachexia models of skeletal muscle"],"prefix":"10.1242","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3662-749X","authenticated-orcid":false,"given":"Fatemeh","family":"Nasehi","sequence":"first","affiliation":[{"name":"Clemson University 1 Department of Bioengineering , , 68 President Street, Charleston, SC 29425 ,","place":["USA"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cameron","family":"Rylance","sequence":"additional","affiliation":[{"name":"Clemson University 1 Department of Bioengineering , , 68 President Street, Charleston, SC 29425 ,","place":["USA"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0009-0004-9730-3661","authenticated-orcid":false,"given":"Erin","family":"Schnell","sequence":"additional","affiliation":[{"name":"University of South Carolina School of Medicine 2 , 6311 Garners Ferry Road, Columbia, SC 29209 ,","place":["USA"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maslyn Ann","family":"Greene","sequence":"additional","affiliation":[{"name":"Clemson University 3 Department of Animal and Veterinary Science , , Lane #129, Clemson, SC 29634 ,","place":["USA"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Caroline","family":"Conway","sequence":"additional","affiliation":[{"name":"Dartmouth's Department of Cognitive Science 4 , 5 Maynard St, Hanover, NH 03755 ,","place":["USA"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zachary","family":"Hough","sequence":"additional","affiliation":[{"name":"University of Maryland, Baltimore School of Medicine 5 , Baltimore, MD 21201 ,","place":["USA"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4057-0062","authenticated-orcid":false,"given":"Susan","family":"Duckett","sequence":"additional","affiliation":[{"name":"Clemson University 3 Department of Animal and Veterinary Science , , Lane #129, Clemson, SC 29634 ,","place":["USA"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8840-4661","authenticated-orcid":false,"given":"Robin C.","family":"Muise-Helmericks","sequence":"additional","affiliation":[{"name":"Medical University of South Carolina 6 Department of Regenerative Medicine and Cell Biology , , 173 Ashley Avenue, Charleston, SC 29425 ,","place":["USA"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3475-8795","authenticated-orcid":false,"given":"Ann Catherine","family":"Foley","sequence":"additional","affiliation":[{"name":"Clemson University 1 Department of Bioengineering , , 68 President Street, Charleston, SC 29425 ,","place":["USA"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"237","published-online":{"date-parts":[[2024,9,25]]},"reference":[{"key":"2024092509050710300_BIO060487C1","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1016\/j.immuni.2011.12.010","article-title":"TAK1 negatively regulates NF-\u03baB and p38 MAP kinase activation in Gr-1+CD11b+ neutrophils","volume":"36","author":"Ajibade","year":"2012","journal-title":"Immunity"},{"key":"2024092509050710300_BIO060487C2","doi-asserted-by":"publisher","first-page":"779","DOI":"10.1007\/s00441-015-2139-2","article-title":"Myostatin induces interstitial fibrosis in the heart via TAK1 and p38","volume":"361","author":"Biesemann","year":"2015","journal-title":"Cell Tissue Res."},{"key":"2024092509050710300_BIO060487C3","doi-asserted-by":"publisher","first-page":"758","DOI":"10.1126\/science.2414846","article-title":"Plasticity of the differentiated state","volume":"230","author":"Blau","year":"1985","journal-title":"Science (New York, N.Y.)"},{"key":"2024092509050710300_BIO060487C4","doi-asserted-by":"publisher","first-page":"e12016","DOI":"10.1371\/journal.pone.0012016","article-title":"A comparative analysis of extra-embryonic endoderm cell lines","volume":"5","author":"Brown","year":"2010","journal-title":"PLoS One"},{"key":"2024092509050710300_BIO060487C5","doi-asserted-by":"publisher","first-page":"e0189818","DOI":"10.1371\/journal.pone.0189818","article-title":"Overexpression of Map3k7 activates sinoatrial node-like differentiation in mouse ES-derived cardiomyocytes","volume":"12","author":"Brown","year":"2017","journal-title":"PLoS 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Microbiol."},{"key":"2024092509050710300_BIO060487C19","doi-asserted-by":"publisher","first-page":"1667","DOI":"10.1038\/cdd.2014.123","article-title":"TAK1 control of cell death","volume":"21","author":"Mihaly","year":"2014","journal-title":"Cell Death Differ."},{"key":"2024092509050710300_BIO060487C20","doi-asserted-by":"publisher","first-page":"151","DOI":"10.1016\/j.devcel.2018.12.002","article-title":"TAK1 prevents endothelial apoptosis and maintains vascular integrity","volume":"48","author":"Naito","year":"2019","journal-title":"Dev. 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