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Early effects of PP60 v‐src kinase activation on caveolae
Author(s) -
Ko YoungGyu,
Liu Pingsheng,
Pathak Ravindra K.,
Craig Leonard C.,
Anderson Richard G. W.
Publication year - 1998
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19981215)71:4<524::aid-jcb7>3.0.co;2-b
Subject(s) - proto oncogene tyrosine protein kinase src , caveolae , kinase , microbiology and biotechnology , chemistry , cancer research , biology , signal transduction
Members of the nonreceptor tyrosine kinase family appear to be targeted to caveolae membrane. We have used a Rat‐1 cell expressing a temperature sensitive pp60 v‐src kinase to assess the initial changes that take place in caveolae after kinase activation. Within 24–48 h after cells were shifted to the permissive temperature, a set of caveolae‐specific proteins became phosphorylated on tyrosine. During this period there was a decline in the caveolae marker protein, caveolin‐1, a loss of invaginated caveolae, and a 70% decline in the sphingomyelin content of the cell. One of the phosphorylated proteins was caveolin‐1 but it was associated in coimmunoprecipitation assays with both a 30 kDa and a 27 kDa tyrosine‐phosphorylated protein. Finally, the cells changed from having a typical fibroblast morphology to a rounded shape lacking polarity. In light of the recent evidence that diverse signaling events originate from caveolae, pp60 v‐src kinase appears to cause global changes to this membrane domain that might directly contribute to the transformed phenotype. J. Cell. Biochem. 71:524–535, 1998. © 1998 Wiley‐Liss, Inc.