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PMID: 9355745 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Protein tyrosine phosphatase 1B interacts with and is tyrosine phosphorylated by the epidermal growth factor receptor.

The Biochemical journal ·Vol. 327 ( Pt 1) ·1997-10-01 ·Pages 139-45

Liu F, Chernoff J

Abstract

We used a substrate-trapping technique to search for substrates of protein tyrosine phosphatase (PTP) 1B. A catalytically inactive form of this enzyme forms a stable, phosphotyrosine-dependent complex with epidermal growth factor receptor (EGFR) both in vitro and in cells. PTP1B also interacts with activated platelet-derived growth factor receptor (PDGFR) but not with colony-stimulating factor 1 receptor (CSF-1R). After binding to EGFR, PTP1B becomes tyrosine-phosphorylated at Tyr-66, a site that conforms to the consensus binding sequence for the Src homology 2 (SH2) domains of the adapter protein Grb2. This tyrosine phosphorylation is correlated with a 3-fold increase in PTP catalytic activity. These findings suggest that PTP1B selectively regulates specific activated receptor protein tyrosine kinases (RPTKs) in vivo and might itself be regulated by such receptors.

MeSH Terms
Animals Blotting, Western COS Cells Electrophoresis, Polyacrylamide Gel Enzyme Activation ErbB Receptors/metabolism Glutathione Transferase/genetics Humans Phosphorylation Phosphotyrosine/metabolism Precipitin Tests Protein Binding Protein Tyrosine Phosphatases/metabolism Receptor Protein-Tyrosine Kinases/metabolism Receptors, Colony-Stimulating Factor/metabolism Receptors, Platelet-Derived Growth Factor/metabolism Recombinant Fusion Proteins/isolation & purification,metabolism Transfection/genetics Tumor Cells, Cultured
Chemicals
Receptors, Colony-Stimulating Factor Recombinant Fusion Proteins Phosphotyrosine Glutathione Transferase ErbB Receptors Receptor Protein-Tyrosine Kinases Receptors, Platelet-Derived Growth Factor Protein Tyrosine Phosphatases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Liu F
Chemistry Department, Temple University, Philadelphia, PA 19122, USA.
Chernoff J
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1997-10-01
Pages
139-45
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1218773
Subset
IM
Grants
NCI NIH HHS · CA58836 · United States
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