| First Author | Klingmüller U | Year | 1995 |
| Journal | Cell | Volume | 80 |
| Issue | 5 | Pages | 729-38 |
| PubMed ID | 7889566 | Mgi Jnum | J:23805 |
| Mgi Id | MGI:71494 | Doi | 10.1016/0092-8674(95)90351-8 |
| Citation | Klingmuller U, et al. (1995) Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell 80(5):729-38 |
| abstractText | The binding of erythropoietin (EPO) to its receptor (EPO-R) activates the protein tyrosine kinase JAK2. The mechanism of JAK2 inactivation has been unclear. We show that the hematopoietic protein tyrosine phosphatase SH-PTP1 (also called HCP and PTP1C) associates via its SH2 domains with the tyrosine-phosphorylated EPO-R. In vitro binding studies suggest that Y429 in the cytoplasmic domain of the EPO-R is the binding site for SH-PTP1. Mutant EPO-Rs lacking Y429 are unable to bind SH-PTP1; cells expressing such mutants are hypersensitive to EPO and display prolonged EPO-induced autophosphorylation of JAK2. Our results suggest that activation of SH-PTP1 by binding to the EPO-R plays a major role in terminating proliferative signals. |
