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Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals
Open accessAbstract
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.
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Wilks, A. F., Harpur, A. G., Kurban, R. R., Ralph, S. J., Zürcher, G., & Ziemiecki, A. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.4.2057 · Cited by 528
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Metadata
- Authors
- Klingmüller, U., Lorenz, U., Cantley, L. C., Neel, B. G., & Lodish, H. F.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1995-03
- Volume
- 80
- Issue
- 5
- Pages
- 729-738
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2100869656
- Cited by
- 929
- References
- 1
- FWCI
- 33.39
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Klingmüller, U., Lorenz, U., Cantley, L. C., Neel, B. G., & Lodish, H. F. (1995). Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell. https://doi.org/10.1016/0092-8674(95)90351-8
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