Unknown

Dataset Information

0

Acetylation of Cavin-1 Promotes Lipolysis in White Adipose Tissue.


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 promoting lipolysis. Our findings shed light on the essential role of cavin-1 in regulating lipolysis in an acetylation-dependent manner in WAT.

SUBMITTER: Zhou SR 

PROVIDER: S-EPMC5533882 | biostudies-other | 2017 Aug

REPOSITORIES: biostudies-other

altmetric image

Publications

Acetylation of Cavin-1 Promotes Lipolysis in White Adipose Tissue.

Zhou Shui-Rong SR   Guo Liang L   Wang Xu X   Liu Yang Y   Peng Wan-Qiu WQ   Liu Yuan Y   Wei Xiang-Bo XB   Dou Xin X   Ding Meng M   Lei Qun-Ying QY   Qian Shu-Wen SW   Li Xi X   Tang Qi-Qun QQ  

Molecular and cellular biology 20170728 16


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 th  ...[more]

Similar Datasets

| S-EPMC9253869 | biostudies-literature
| S-EPMC4818253 | biostudies-literature
| S-EPMC4175185 | biostudies-literature
| S-EPMC9576180 | biostudies-literature
| S-EPMC4109056 | biostudies-literature
| S-EPMC5181317 | biostudies-literature
| S-EPMC4112219 | biostudies-literature
| S-EPMC7322621 | biostudies-literature
| S-EPMC7707166 | biostudies-literature
| S-EPMC6309263 | biostudies-literature