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
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
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DOI:
10.1073/pnas.90.15.6939
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发表时间:
1993-08-01
影响因子:
11.1
通讯作者:
VALIUS, M
中科院分区:
文献类型:
--
作者:
KAZLAUSKAS, A;FENG, GS;VALIUS, M
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.