Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals
摘要：
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 PTPIC) 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.
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关键词：
Animals B-Lymphocytes Bone Marrow Cells Cell Division Cell Line Cytoplasm Enzyme Activation Erythropoietin Intracellular Signaling Peptides and Proteins Janus Kinase 2
DOI：
10.1016/0092-8674(95)90351-8
被引量：
年份：
1995
Taylor & Francis
Elsevier
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BMJ
万方医学
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