FEBS Letters | |
Phosphorylation and dephosphorylation of hormone‐sensitive lipase Interactions between the regulatory and basal phosphorylation sites | |
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
【 预 览 】
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RO201912020290539ZK.pdf | 426KB | download |