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Hematopoietic cell phosphatase associates with erythropoietin (Epo)
receptor after Epo-induced receptor tyrosine phosphorylation:
identification of potential binding sites
T Yi, J Zhang, O Miura and JN Ihle
Department of Cancer Biology, Cleveland Clinic Foundation Research
Institute, OH.
Erythropoietin (Epo) binding to its receptor (EpoR) induces tyrosine
phosphorylation in responsive cells and this ability is required for a
mitogenic response. One of the substrates of tyrosine phosphorylation is
the Epo receptor (EpoR). The carboxyl region of EpoR cytoplasmic domain is
required for EpoR phosphorylation and has been shown to negatively affect
the response to Epo both in vivo and in cell lines. Hematopoietic cell
phosphatase (HCP) has also been hypothesized to negatively regulate
erythropoiesis, based on the hypersensitivity to Epo of erythroid lineage
cells in moth-eaten mice that genetically lack HCP. In the studies
presented here, we show that HCP binds the tyrosine phosphorylated Epo
receptor through the amino-terminal src-homology 2 (SH2) domain of HCP.
Using a series of phosphotyrosine-containing peptides, potential HCP
binding sites in the cytoplasmic domain of the EpoR are identified. The
results support the concept that, after Epo stimulation, phosphorylation of
EpoR provides a docking site for HCP in the receptor complex. Recruitment
of HCP to the complex and its subsequent dephosphorylation of substrates
and/or associated kinases may be important to mitigate the ligand-induced
mitogenic response.
Volume 85,
Issue 1,
pp. 87-95,
01/01/1995
Copyright © 1995 by The American Society of Hematology
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