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rdf:type |
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lifeskim:mentions |
umls-concept:C0015127,
umls-concept:C0059570,
umls-concept:C0205369,
umls-concept:C0271510,
umls-concept:C0334094,
umls-concept:C1314792,
umls-concept:C1334291,
umls-concept:C1549081,
umls-concept:C1692758,
umls-concept:C1705637,
umls-concept:C1710082
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pubmed:issue |
5
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pubmed:dateCreated |
1995-4-14
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pubmed: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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Erythropoietin,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Jak2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Janus Kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ptpn11 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ptpn6 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Erythropoietin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
80
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
729-38
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7889566-Animals,
pubmed-meshheading:7889566-B-Lymphocytes,
pubmed-meshheading:7889566-Bone Marrow Cells,
pubmed-meshheading:7889566-Cell Division,
pubmed-meshheading:7889566-Cell Line,
pubmed-meshheading:7889566-Cytoplasm,
pubmed-meshheading:7889566-Enzyme Activation,
pubmed-meshheading:7889566-Erythropoietin,
pubmed-meshheading:7889566-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:7889566-Janus Kinase 2,
pubmed-meshheading:7889566-Mice,
pubmed-meshheading:7889566-Phosphorylation,
pubmed-meshheading:7889566-Point Mutation,
pubmed-meshheading:7889566-Protein Tyrosine Phosphatase, Non-Receptor Type 11,
pubmed-meshheading:7889566-Protein Tyrosine Phosphatase, Non-Receptor Type 6,
pubmed-meshheading:7889566-Protein Tyrosine Phosphatases,
pubmed-meshheading:7889566-Protein-Tyrosine Kinases,
pubmed-meshheading:7889566-Proto-Oncogene Proteins,
pubmed-meshheading:7889566-Receptors, Erythropoietin,
pubmed-meshheading:7889566-Recombinant Fusion Proteins,
pubmed-meshheading:7889566-Signal Transduction,
pubmed-meshheading:7889566-Tyrosine
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pubmed:year |
1995
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pubmed:articleTitle |
Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals.
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pubmed:affiliation |
Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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