IDENTIFICATION AND ROLE OF THE BASAL PHOSPHORYLATION SITE ON HORMONE-SENSITIVE LIPASE

被引：104

作者：

GARTON, AJ ^{[1
]}

YEAMAN, SJ ^{[1
]}

机构：

[1] UNIV NEWCASTLE UPON TYNE,SCH MED,DEPT BIOCHEM & GENET,NEWCASTLE TYNE NE2 4HH,ENGLAND

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1990年 / 191卷 / 01期

关键词：

D O I：

10.1111/j.1432-1033.1990.tb19116.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 at site 2 totally prevents the subsequent phosphorylation of site 1 and vice versa. Copyright © 1990, Wiley Blackwell. All rights reserved

引用

页码：245 / 250

页数：6

共 27 条

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