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Reassessing the Role of Phosphocaveolin‐1 in Cell Adhesion and Migration
Author(s) -
Hill Michelle M.,
Scherbakov Nadja,
Schiefermeier Natalia,
Baran JoAnne,
Hancock John F.,
Huber Lukas A.,
Parton Robert G.,
Parat MarieOdile
Publication year - 2007
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2007.00653.x
Subject(s) - paxillin , biology , focal adhesion , immunostaining , tyrosine phosphorylation , cell adhesion , microbiology and biotechnology , cell migration , phosphorylation , monoclonal antibody , adhesion , tyrosine , antibody , cell , immunology , biochemistry , immunohistochemistry , chemistry , organic chemistry
Although phosphorylation on tyrosine 14 was identified early in the discovery of caveolin‐1, the functional significance of this modification still remains elusive. Recent evidence points to a role of caveolin‐1 tyrosine 14 phosphorylation in cell adhesion and migration. These results are based on a variety of tools, including a widely used mouse monoclonal anti‐phosphocaveolin‐1 antibody, which labels, in cultured cells, a protein localized at or near focal adhesions. We here report results from three independent laboratories, showing that this antibody recognizes phosphocaveolin‐1 amongst other proteins in immunoblot analyses and that the signal obtained with this antibody in immunostaining experiments is in part due to labeling of paxillin. Published data need to be interpreted keeping in mind that images of phosphocaveolin‐1 cellular localization obtained using this antibody are not valid. We re‐evaluate the current knowledge about the role of caveolin‐1 in cell adhesion and migration in view of this new information.