Literature DB >> 2537200

Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism.

A J Garton1, D G Campbell, D Carling, D G Hardie, R J Colbran, S J Yeaman.   

Abstract

Hormone-sensitive lipase is phosphorylated at a single site (site 2) in vitro by the AMP-activated protein kinase, without any direct effect on the activity of the enzyme. The amino acid sequence around this site has been determined. Ca2+/calmodulin-dependent protein kinase II also phosphorylates hormone-sensitive lipase predominantly at this site, whilst cyclic-GMP-dependent protein kinase phosphorylates exclusively the regulatory site (site 1) which is also phosphorylated by cyclic-AMP-dependent protein kinase. Phosphorylation of site 2 has been found to inhibit subsequent phosphorylation and activation of hormone-sensitive lipase by the cyclic-AMP-dependent and cyclic-GMP-dependent protein kinases, indicating that site-2 phosphorylation may have an antilipolytic role in vivo.

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Year:  1989        PMID: 2537200     DOI: 10.1111/j.1432-1033.1989.tb14548.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  65 in total

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8.  Mechanism of hormone-stimulated lipolysis in adipocytes: translocation of hormone-sensitive lipase to the lipid storage droplet.

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Journal:  Br J Pharmacol       Date:  2008-02-25       Impact factor: 8.739

10.  PKA phosphorylates and inactivates AMPKalpha to promote efficient lipolysis.

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Journal:  EMBO J       Date:  2009-11-26       Impact factor: 11.598

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