N-terminal processing and modifications of caveolin-1 in caveolae from human adipocytes

Biochemical and Biophysical Research Communications
Julia P VainonenAlexander V Vener

Abstract

Caveolin, the principal structural protein of caveolae membrane domains, has a cytosol-exposed N-terminal part that was cleaved off by trypsin treatment of caveolae vesicles isolated from primary human adipocytes. Sequencing of the released tryptic peptides by nanospray quadrupole time-of-flight mass spectrometry revealed that both caveolin-1alpha and caveolin-1beta were processed by excision of the starting methionines. The N-terminus of the mature caveolin-1alpha was acetylated, while caveolin-1beta was found in acetylated as well as in non-acetylated forms. Fractional phosphorylation of serine-36 in the mature caveolin-1alpha and of the homologous serine-5 in caveolin-1beta was identified. This is the first experimental evidence for in vivo phosphorylation of caveolin-1 at the consensus site for phosphorylation by protein kinase C. The phosphorylation was found in both the acetylated and non-acetylated variants of caveolin-1beta. This variability in modifications is consistent with critical involvement of the N-terminal domain of caveolin in the regulation of caveolae.

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Citations

Jul 14, 2005·IUBMB Life·Alexander V Vener, Peter Strålfors
Oct 5, 2006·Molecular & Cellular Proteomics : MCP·Sanjin ZvonicJeffrey M Gimble
Sep 26, 2019·Biochemical Society Transactions·Kyle T RootKerney Jebrell Glover
Mar 11, 2006·The Journal of Biological Chemistry·Nabila AboulaichPeter Strålfors
Sep 10, 2021·Journal of Cancer Research and Clinical Oncology·Xingning LaiLixia Xiong

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