کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1936585 | 1050695 | 2008 | 7 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Proteomic identification of ZO-1/2 as a novel scaffold for Src/Csk regulatory circuit Proteomic identification of ZO-1/2 as a novel scaffold for Src/Csk regulatory circuit](/preview/png/1936585.png)
To elucidate the regulatory mechanism of cell transformation induced by c-Src tyrosine kinase, we performed a proteomic analysis of tyrosine phosphorylated proteins that interact with c-Src and/or its negative regulator Csk. The c-Src interacting proteins were affinity-purified from Src transformed cells using the Src SH2 domain as a ligand. LC–MS/MS analysis of the purified proteins identified general Src substrates, such as focal adhesion kinase and paxillin, and ZO-1/2 as a transformation-dependent Src target. The Csk binding proteins were analyzed by a tandem affinity purification method. In addition to the previously identified Csk binding proteins, including Cbp/PAG, paxillin, and caveolin-1, we found that ZO-1/2 could also serve as a major Csk binding protein. ZO-2 was phosphorylated concurrently with Src transformation and specifically bound to Csk in a Csk SH2 dependent manner. These results suggest novel roles for ZO proteins as Src/Csk scaffolds potentially involved in the regulation of Src transformation.
Journal: Biochemical and Biophysical Research Communications - Volume 366, Issue 4, 22 February 2008, Pages 969–975