| First Author | Watanabe N | Year | 2005 |
| Journal | Mol Cell Biochem | Volume | 269 |
| Issue | 1-2 | Pages | 13-7 |
| PubMed ID | 15786712 | Mgi Jnum | J:180575 |
| Mgi Id | MGI:5306581 | Doi | 10.1007/s11010-005-2149-6 |
| Citation | Watanabe N, et al. (2005) Leupaxin binds to PEST domain tyrosine phosphatase PEP. Mol Cell Biochem 269(1-2):13-7 |
| abstractText | PEST domain tyrosine phosphatase (PEP) is an intracellular protein tyrosine phosphatase and characterized by PEST motifs and proline-rich domains in the carboxyl terminal half. PEP is primarily expressed in hematopoietic cells, and together with PEP-binding Csk, may act as a negative regulator of antigen receptor signaling in lymphocytes. Here, we show the binding capability of PEP for leupaxin, which is preferentially expressed in hematopoietic cells and a comparatively new member of the paxillin family characterized by two protein-protein interaction modules, LIM domains and LD motifs. These results suggested that leupaxin might participate in the regulation of the signaling cascade through the binding to PEP in lymphocytes. |
