{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T12:02:28Z","timestamp":1788436948508,"version":"build-2803163510"},"reference-count":38,"publisher":"Wiley","issue":"19","license":[{"start":{"date-parts":[[2025,9,12]],"date-time":"2025-09-12T00:00:00Z","timestamp":1757635200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[2025,10]]},"abstract":"<jats:sec>\n                    <jats:label\/>\n                    <jats:p>\n                      Acyl\u2010coenzyme A synthetase short\u2010chain family member\u20102 (ACSS2) catalyzes the conversion of acetate to acetyl\u2010CoA, regulating cholesterol metabolism. Given the discovery of a muscular dystrophy associated with 3\u2010hydroxy\u20103\u2010methyl\u2010glutaryl\u2010coenzyme A reductase (HMGCR), a key enzyme in cholesterol synthesis, we studied\n                      <jats:italic>Acss2<\/jats:italic>\n                      in mice and the orthologous gene\n                      <jats:italic>AcCoA<\/jats:italic>\n                      in flies. Skeletal muscle from\n                      <jats:italic>Acss2<\/jats:italic>\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      mice showed atrophic fibers, lipid accumulation, and depleted NADH levels, while myoblasts from these mice displayed precocious differentiation. Exercise induced fatigue in the\n                      <jats:italic>Acss2<\/jats:italic>\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      mice, which was accentuated by inhibition of ATP\u2010citrate lyase (ACLY) activity.\n                      <jats:italic>AcCoA<\/jats:italic>\n                      knockdown yielded reduced body sizes and locomotor defects in\n                      <jats:italic>Drosophila<\/jats:italic>\n                      . ACSS2 is vital for skeletal muscle function and merits study as a potential factor in muscle diseases related to cholesterol metabolism.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:label\/>\n                    <jats:p>\n                      <jats:boxed-text content-type=\"box\" position=\"anchor\">\n                        <jats:caption>\n                          <jats:title>Impact statement<\/jats:title>\n                        <\/jats:caption>\n                        <jats:p>ACSS2 catalyzes the conversion of acetate to acetyl\u2010CoA, regulating cholesterol metabolism. Given the increasingly apparent links between cholesterol metabolism and skeletal muscle function, we investigated ACSS2 deficiency in mouse and fly models. We identified defects in muscle morphology, muscle metabolism, and motor function. ACSS2 is vital for skeletal muscle.<\/jats:p>\n                      <\/jats:boxed-text>\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1002\/1873-3468.70152","type":"journal-article","created":{"date-parts":[[2025,9,12]],"date-time":"2025-09-12T07:36:44Z","timestamp":1757662604000},"page":"2817-2827","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["<scp>ACSS2<\/scp>\n                    involved in acetyl\u2010\n                    <scp>CoA<\/scp>\n                    synthesis regulates skeletal muscle function"],"prefix":"10.1002","volume":"599","author":[{"given":"Mekala","family":"Gunasekaran","sequence":"first","affiliation":[{"name":"Greg Marzolf Jr. Muscular Dystrophy Center and Department of Neurology University of Minnesota Medical School  Minneapolis MN 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