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Endogenous and Synthetic ABHD5 Ligands Regulate ABHD5-Perilipin Interactions and Lipolysis in Fat and Muscle.

Abstract：

:Fat and muscle lipolysis involves functional interactions of adipose triglyceride lipase (ATGL), α-β hydrolase domain-containing protein 5 (ABHD5), and tissue-specific perilipins 1 and 5 (PLIN1 and PLIN5). ABHD5 potently activates ATGL, but this lipase-promoting activity is suppressed when ABHD5 is bound to PLIN proteins on lipid droplets. In adipocytes, protein kinase A (PKA) phosphorylation of PLIN1 rapidly releases ABHD5 to activate ATGL, but mechanisms for rapid regulation of PLIN5-ABHD5 interaction in muscle are unknown. Here, we identify synthetic ligands that release ABHD5 from PLIN1 or PLIN5 without PKA activation and rapidly activate adipocyte and muscle lipolysis. Molecular imaging and affinity probe labeling demonstrated that ABHD5 is directly targeted by these synthetic ligands and additionally revealed that ABHD5-PLIN interactions are regulated by endogenous ligands, including long-chain acyl-CoA. Our results reveal a new locus of lipolysis control and suggest ABHD5 ligands might be developed into novel therapeutics that directly promote fat catabolism.

journal_name

Cell Metab

journal_title

Cell metabolism

authors

Sanders MA,Madoux F,Mladenovic L,Zhang H,Ye X,Angrish M,Mottillo EP,Caruso JA,Halvorsen G,Roush WR,Chase P,Hodder P,Granneman JG

doi

10.1016/j.cmet.2015.08.023

subject

Has Abstract

pub_date

2015-11-03 00:00:00

pages

851-60

issue

5

eissn

1550-4131

issn

1932-7420

pii

S1550-4131(15)00456-8

journal_volume

22

pub_type

杂志文章

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