Identification and role of the basal phosphorylation site on hormone‐sensitive lipase
- 1 July 1990
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 191 (1) , 245-250
- https://doi.org/10.1111/j.1432-1033.1990.tb19116.x
Abstract
Phosphorylation site 2 on bovine hormone-sensitive lipase (HSL), which is phosphorylated in vitro by the AMP-activated protein kinase, has been found also to be phosphorylated in vitro by glycogen synthase kinase-4. Peptide mapping of HSL phosphorylated in vitro and in isolated adipocytes demonstrates that this site corresponds to the basal phosphorylation site on HSL, which is phosphorylated in intact adipocytes in the absence of lipolytic stimuli. Site 2 has been proposed to have an antilipolytic role in that phosphorylation at this site greatly reduces subsequent phosphorylation (at site 1) and activation of HSL by cyclic-AMP-dependent protein kinase. Further evidence for an antilipolytic role of site 2 has been obtained using a synthetic peptide based on the sequence around sites 1 and 2. Phosphorylation of the peptide as site 2 totally prevents the subsequent phosphorylation of site 1 and vice versa.This publication has 28 references indexed in Scilit:
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