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The phosphorylation of caveolin-2 on serines 23 and 36 modulates caveolin-1-dependent caveolae formation.

Authors: Sowa, G  Pypaert, M  Fulton, D  Sessa, WC 
Citation: Sowa G, etal., Proc Natl Acad Sci U S A. 2003 May 27;100(11):6511-6. Epub 2003 May 12.
Pubmed: (View Article at PubMed) PMID:12743374
DOI: Full-text: DOI:10.1073/pnas.1031672100

Caveolin-1 and -2 are the two major coat proteins found in plasma membrane caveolae of most of cell types. Here, by using adenoviral transduction of either caveolin-1 or caveolin-2 or both isoforms into cells lacking both caveolins, we demonstrate that caveolin-2 positively regulates caveolin-1-dependent caveolae formation. More importantly, we show that caveolin-2 is phosphorylated in vivo at two serine residues and that the phosphorylation of caveolin-2 is necessary for its actions as a positive regulator of caveolin-1 during organelle biogenesis in prostate cancer cells. Mutation of the primary phosphorylation sites on caveolin-2, serine 23 and 36, reduces the number of plasmalemma-attached caveolae and increases the accumulation of noncoated vesicles, but does not affect trafficking of caveolin-2, interaction with caveolin-1 or its biophysical properties. Thus, the phosphorylation of caveolin-2 is a novel mechanism to regulate the dynamics of caveolae assembly.


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CRRD Object Information
CRRD ID: 8554755
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE


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