{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,27]],"date-time":"2026-02-27T01:32:12Z","timestamp":1772155932467,"version":"3.50.1"},"reference-count":35,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2023,9,24]],"date-time":"2023-09-24T00:00:00Z","timestamp":1695513600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["5T32NS095775"],"award-info":[{"award-number":["5T32NS095775"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[2023,10]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    DOCK (dedicator of cytokinesis) is an 11\u2010member family of typical guanine nucleotide exchange factors (GEFs) expressed in the brain, spinal cord, and skeletal muscle. Several DOCK proteins have been implicated in maintaining several myogenic processes such as fusion. We previously identified DOCK3 as being strongly upregulated in Duchenne muscular dystrophy (DMD), specifically in the skeletal muscles of DMD patients and dystrophic mice.\n                    <jats:italic>Dock3<\/jats:italic>\n                    ubiquitous KO mice on the dystrophin\u2010deficient background exacerbated skeletal muscle and cardiac phenotypes. We generated\n                    <jats:italic>Dock3<\/jats:italic>\n                    conditional skeletal muscle knockout mice (\n                    <jats:italic>Dock3<\/jats:italic>\n                    mKO) to characterize the role of DOCK3 protein exclusively in the adult muscle lineage.\n                    <jats:italic>Dock3<\/jats:italic>\n                    mKO mice presented with significant hyperglycemia and increased fat mass, indicating a metabolic role in the maintenance of skeletal muscle health.\n                    <jats:italic>Dock3<\/jats:italic>\n                    mKO mice had impaired muscle architecture, reduced locomotor activity, impaired myofiber regeneration, and metabolic dysfunction. We identified a novel DOCK3 interaction with SORBS1 through the C\u2010terminal domain of DOCK3 that may account for its metabolic dysregulation. Together, these findings demonstrate an essential role for DOCK3 in skeletal muscle independent of DOCK3 function in neuronal lineages.\n                  <\/jats:p>","DOI":"10.1096\/fj.202300386rr","type":"journal-article","created":{"date-parts":[[2023,9,24]],"date-time":"2023-09-24T09:59:50Z","timestamp":1695549590000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["<scp>DOCK3<\/scp>\n                    regulates normal skeletal muscle regeneration and glucose metabolism"],"prefix":"10.1096","volume":"37","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4361-5008","authenticated-orcid":false,"given":"Adrienne","family":"Samani","sequence":"first","affiliation":[{"name":"Division of Neurology, Department of Pediatrics University of Alabama at Birmingham and Children's of Alabama  Birmingham Alabama 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