Blog
About

7
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Src family kinase-dependent phosphorylation of a 29-kDa caveolin-associated protein.

      Biochemical and Biophysical Research Communications

      metabolism, src-Family Kinases, genetics, Substrate Specificity, Proto-Oncogene Proteins c-fyn, physiology, biosynthesis, Proto-Oncogene Proteins, pharmacology, antagonists & inhibitors, Platelet-Derived Growth Factor, Phosphorylation, Phosphoproteins, Molecular Weight, Mice, Humans, Genetic Vectors, Cell Line, Caveolins, Caveolin 1, enzymology, Caveolae, Animals, 3T3 Cells

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          PDGF receptors and Src family kinases are concentrated in caveolae, where signal transduction cascades involving these molecules are thought to be organized. The Src family tyrosine kinases are cotransducers of signals emanating from the activated PDGF receptor. However, the Src family kinase substrates that are involved in PDGF-induced signaling remain to be fully elucidated. We have identified a 29-kDa protein in caveolae that was phosphorylated in response to PDGF stimulation. This protein, pp29, was tightly bound to the caveolar coat protein caveolin-1. pp29 was among the most prominent phosphoproteins observed in cells overexpressing Fyn, suggesting that it may be a Fyn substrate. Consistent with this, pp29 was among a specific subset of proteins whose PDGF-stimulated phosphorylation was blocked by expression of kinase inactive Fyn. These data indicate that pp29 lies downstream of Fyn activation in a PDGF-stimulated signaling pathway, and that pp29 is an abundant site for nucleation of signal transduction cascades. ©2002 Elsevier Science (USA).

          Related collections

          Author and article information

          Journal
          10.1006/bbrc.2002.6371
          11820784

          Comments

          Comment on this article