Phosphorylation and dephosphorylation of hormone‐sensitive lipase Interactions between the regulatory and basal phosphorylation sites

FEBS Letters

Belfrage, Per¹  Olsson, Håkan¹ 

[1] Department of Medical and Physiological Chemistry 4, University of Lund, Lund, Sweden

关键词: Hormone-sensitive lipase;    cyclic AMP-dependent protein kinase;    Protein phosphatase;    Glycogen synthase kinase-4;    Phosphorylation site;    SDS-PAGE;    polyacrylamide gel electrophoresis in the presence of SDS;    C12E8;    octaethylene glycol dodecylmonoether;   

DOI  :  10.1016/0014-5793(88)80390-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phosphorylation of the basal site with glycogen synthase kinase-4 enhanced the rate of phosphorylation of the regulatory site by cyclic AMP-dependent protein kinase 1.7-fold. In contrast, the phosphorylation state of the regulatory site did not affect the rate of phosphorylation of the basal site with glycogen synthase kinase-4. The rate of dephosphorylation of either the regulatory or the basal phosphorylation site by protein phosphatase-1, 2A or 2C was independent of the phosphorylation state of the other site. These results suggest that the basal phosphorylation site could play an indirect role in the control of the hormone-sensitive lipase activity in the adipocyte by functioning as a recognition site for the cyclic AMP-dependent protein kinase in the phosphorylation of the activity-controlling regulatory phosphorylation site in response to lipolytic hormones.

【 授权许可】

Unknown