| First Author | Saito K | Year | 2008 |
| Journal | Biochem Biophys Res Commun | Volume | 366 |
| Issue | 4 | Pages | 969-75 |
| PubMed ID | 18086565 | Mgi Jnum | J:130803 |
| Mgi Id | MGI:3772378 | Doi | 10.1016/j.bbrc.2007.12.055 |
| Citation | Saito K, et al. (2008) Proteomic identification of ZO-1/2 as a novel scaffold for Src/Csk regulatory circuit. Biochem Biophys Res Commun 366(4):969-75 |
| abstractText | 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. |
