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PMID: 7688466 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 90 ·No. 15 ·1993-08-01 ·Pages 6939-43

Kazlauskas A, Feng GS, Pawson T, Valius M

Abstract

Ligand-stimulated autophosphorylation of the platelet-derived growth factor receptor (PDGFR) beta subunit creates a number of binding sites for SH2-containing proteins. One of the PDGFR-associated proteins is a 64-kDa protein of unknown identity and function. We present data indicating that the 64-kDa protein that associates with the activated PDGFR is Syp (also called SH-PTP2, PTP-1D, or SH-PTP3), the ubiquitously expressed 64-kDa SH2-containing protein-tyrosine phosphatase. Phosphorylation of Tyr-1009 in the C terminus of the PDGFR is required for the stable association of Syp, suggesting that phosphorylation of this residue creates a binding site for the Syp SH2 domains. Although Syp stably associates with the PDGFR, this event is not required for PDGF-stimulated tyrosine phosphorylation of Syp. These data raise the interesting possibility that protein-tyrosine phosphatases contribute to the intracellular relay of biological signals originating from receptor tyrosine kinases such as the PDGFR.

Related Genes
PDGFR Syp
MeSH Terms
Humans In Vitro Techniques Intracellular Signaling Peptides and Proteins Macromolecular Substances Peptide Mapping Phosphorylation Phosphotyrosine Protein Binding Protein Tyrosine Phosphatase, Non-Receptor Type 11 Protein Tyrosine Phosphatase, Non-Receptor Type 6 Protein Tyrosine Phosphatases/metabolism Receptors, Platelet-Derived Growth Factor/metabolism Tumor Cells, Cultured Tyrosine/analogs & derivatives,metabolism
Chemicals
Intracellular Signaling Peptides and Proteins Macromolecular Substances Phosphotyrosine Tyrosine Receptors, Platelet-Derived Growth Factor PTPN11 protein, human PTPN6 protein, human Protein Tyrosine Phosphatase, Non-Receptor Type 11 Protein Tyrosine Phosphatase, Non-Receptor Type 6 Protein Tyrosine Phosphatases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Kazlauskas A
National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206.
Feng G S
Pawson T
Valius M
References (41)
41 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.90.15.6939
Published
1993-08-01
Pages
6939-43
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC47050
Subset
IM
Grants
NCI NIH HHS · CA55063 · United States
NIGMS NIH HHS · GM48339 · United States
External Links
PubMed source DOI: 10.1073/pnas.90.15.6939 PMC Full Text View journal details
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