{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhou SR"],"funding":["National Natural Science Foundation of China Grant","National Natural Science Foundation of China","985 Project","Shanghai Leading Academic Discipline Project","National Key Basic Research Project Grant"],"pagination":["e00058-17"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5533882"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["37(16)"],"pubmed_abstract":["White adipose tissue (WAT) serves as a reversible energy storage depot in the form of lipids in response to nutritional status. Cavin-1, an essential component in the biogenesis of caveolae, is a positive regulator of lipolysis in adipocytes. However, molecular mechanisms of cavin-1 in the modulation of lipolysis remain poorly understood. Here, we showed that cavin-1 was acetylated at lysines 291, 293, and 298 (3K), which were under nutritional regulation in WAT. We further identified GCN5 as the acetyltransferase and Sirt1 as the deacetylase of cavin-1. Acetylation-mimetic 3Q mutants of cavin-1 augmented fat mobilization in 3T3-L1 adipocytes and zebrafish. Mechanistically, acetylated cavin-1 preferentially interacted with hormone-sensitive lipase and recruited it to the caveolae, thereby "],"journal":["Molecular and cellular biology"],"pubmed_title":["Acetylation of Cavin-1 Promotes Lipolysis in White Adipose Tissue."],"pmcid":["PMC5533882"],"funding_grant_id":["2013CB530601","B110","31571471","985 III-YFX0302","81601251","31370027","81390350","2011CB910201"],"pubmed_authors":["Dou X","Qian SW","Zhou SR","Liu Y","Li X","Guo L","Tang QQ","Peng WQ","Lei QY","Wei XB","Wang X","Ding M"],"additional_accession":[]},"is_claimable":false,"name":"Acetylation of Cavin-1 Promotes Lipolysis in White Adipose Tissue.","description":"White adipose tissue (WAT) serves as a reversible energy storage depot in the form of lipids in response to nutritional status. Cavin-1, an essential component in the biogenesis of caveolae, is a positive regulator of lipolysis in adipocytes. However, molecular mechanisms of cavin-1 in the modulation of lipolysis remain poorly understood. Here, we showed that cavin-1 was acetylated at lysines 291, 293, and 298 (3K), which were under nutritional regulation in WAT. We further identified GCN5 as the acetyltransferase and Sirt1 as the deacetylase of cavin-1. Acetylation-mimetic 3Q mutants of cavin-1 augmented fat mobilization in 3T3-L1 adipocytes and zebrafish. Mechanistically, acetylated cavin-1 preferentially interacted with hormone-sensitive lipase and recruited it to the caveolae, thereby ","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Aug","modification":"2025-04-26T08:51:57.964Z","creation":"2019-03-26T22:58:44Z"},"accession":"S-EPMC5533882","cross_references":{"pubmed":["28559430"],"doi":["10.1128/mcb.00058-17","10.1128/MCB.00058-17"]}}