| First Author | Lu W | Year | 2001 |
| Journal | Mol Cell | Volume | 8 |
| Issue | 4 | Pages | 759-69 |
| PubMed ID | 11684012 | Mgi Jnum | J:200332 |
| Mgi Id | MGI:5508291 | Doi | 10.1016/s1097-2765(01)00369-0 |
| Citation | Lu W, et al. (2001) Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling. Mol Cell 8(4):759-69 |
| abstractText | The regulation of protein tyrosine phosphatase (PTPase) SHP-2 is proposed to involve tyrosine phosphorylation on two tail tyrosine residues. Using "expressed protein ligation", nonhydrolyzable phosphotyrosine analogs were introduced at known phosphorylation sites in SHP-2. Biochemical analysis suggests that a phosphonate at Tyr542 interacts intramolecularly with the N-terminal SH2 domain to relieve basal inhibition of the PTPase, whereas a phosphonate at Tyr-580 stimulates the PTPase activity by interaction with the C-terminal SH2 domain. Microinjection experiments indicate that a single phosphorylation of Tyr-542 of SHP-2 is sufficient to activate the MAP kinase pathway in living cells. These studies support a novel mechanism explaining how tyrosine phosphorylation of a PTPase is important in signal transduction. |
