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Dysregulation of fatty acid (FA) metabolism is associated with MM development and progression; however, the underlying mechanisms remain unclear. Herein, we explore the roles of long\u2010chain fatty acid coenzyme A ligase (ACSL) family members in MM. ACSLs convert free long\u2010chain fatty acids into fatty acyl\u2010CoA esters and play key roles in catabolic and anabolic fatty acid metabolism. Analysis of the Multiple Myeloma Research Foundation (MMRF) CoMMpass\n                    <jats:sup>SM<\/jats:sup>\n                    study showed that high\n                    <jats:italic>ACSL1<\/jats:italic>\n                    and\n                    <jats:italic>ACSL4<\/jats:italic>\n                    expression in myeloma cells are both associated with worse clinical outcomes for MM patients. Cancer Dependency Map (DepMap) data showed that all five ACSLs have negative Chronos scores, and\n                    <jats:italic>ACSL3<\/jats:italic>\n                    and\n                    <jats:italic>ACSL4<\/jats:italic>\n                    were among the top 25% Hallmark Fatty Acid Metabolism genes that support myeloma cell line fitness. Inhibition of ACSLs in myeloma cell lines\n                    <jats:italic>in vitro<\/jats:italic>\n                    , using the pharmacological inhibitor Triacsin C (TriC), increased apoptosis, decreased proliferation, and decreased cell viability, in a dose\u2010 and time\u2010dependent manner. RNA\u2010sequencing analysis of MM.1S cells treated with TriC showed a significant enrichment in apoptosis, ferroptosis, and endoplasmic reticulum (ER) stress, and proteomic analysis of these cells revealed enriched pathways for mitochondrial dysfunction and oxidative phosphorylation. TriC also rewired mitochondrial metabolism by decreasing mitochondrial membrane potential, increasing mitochondrial superoxide levels, decreasing mitochondrial ATP production rates, and impairing cellular respiration. Overall, our data support the hypothesis that suppression of ACSLs in myeloma cells is a novel metabolic target in MM that inhibits their viability, implicating this family as a promising therapeutic target in treating myeloma.\n                  <\/jats:p>","DOI":"10.1002\/1878-0261.13794","type":"journal-article","created":{"date-parts":[[2025,1,23]],"date-time":"2025-01-23T12:38:44Z","timestamp":1737635924000},"page":"1687-1706","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Inhibition of acyl\u2010\n                    <scp>CoA<\/scp>\n                    synthetase long\u2010chain isozymes decreases multiple myeloma cell proliferation and causes mitochondrial dysfunction"],"prefix":"10.1002","volume":"19","author":[{"given":"Connor S.","family":"Murphy","sequence":"first","affiliation":[{"name":"Center for Molecular Medicine MaineHealth Institute for Research  Scarborough ME USA"},{"name":"University of Maine Graduate School of Biomedical Science and Engineering University of Maine  Orono ME USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Heather","family":"Fairfield","sequence":"additional","affiliation":[{"name":"Center for Molecular Medicine MaineHealth Institute for Research  Scarborough ME USA"},{"name":"School of Medicine Tufts University  Boston MA USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Victoria E.","family":"DeMambro","sequence":"additional","affiliation":[{"name":"Center for Molecular Medicine MaineHealth Institute for Research  Scarborough ME USA"},{"name":"University of Maine Graduate School of Biomedical Science and Engineering University of Maine  Orono ME USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Samaa","family":"Fadel","sequence":"additional","affiliation":[{"name":"Center for Molecular Medicine MaineHealth Institute for Research  Scarborough ME USA"},{"name":"School of Medicine Tufts University  Boston MA USA"},{"name":"University of New England  Biddeford ME USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carlos A.","family":"Gartner","sequence":"additional","affiliation":[{"name":"Center for Molecular Medicine MaineHealth Institute for Research  Scarborough ME USA"},{"name":"University of Maine Graduate School of Biomedical Science and Engineering University of Maine  Orono ME USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michelle","family":"Karam","sequence":"additional","affiliation":[{"name":"Center for Molecular Medicine MaineHealth Institute for Research  Scarborough ME USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Potts","sequence":"additional","affiliation":[{"name":"Center for Molecular Medicine MaineHealth Institute for Research  Scarborough ME USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Princess","family":"Rodriguez","sequence":"additional","affiliation":[{"name":"Vermont Integrative Genomics Resource DNA Facility University of Vermont  Burlington VT USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ya\u2010Wei","family":"Qiang","sequence":"additional","affiliation":[{"name":"Center for Molecular Medicine MaineHealth Institute for Research  Scarborough ME USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Habib","family":"Hamidi","sequence":"additional","affiliation":[{"name":"Genentech, Inc.  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