Identification of the major SHPTP2-binding protein that is tyrosine-phosphorylated in response to insulin.

doi:10.1074/jbc.270.30.17716

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Article

Identification of the major SHPTP2-binding protein that is tyrosine-phosphorylated in response to insulin.

The Journal of biological chemistry - 28 Jul 1995

Yamauchi K, Ribon V, Saltiel A R, Pessin J E

Abstract excerpt

Immunoprecipitation of the cytosolic Src homology 2 domain-containing protein-tyrosine phosphatase, SHPTP2, from insulin-stimulated 3T3L1 adipocytes or Chinese hamster ovary cells expressing the human insulin receptor resulted in the coimmunoprecipitation of a diffuse tyrosine-phosphorylated band in the 115-kDa protein region on SDS-polyacrylamide gels. Although platelet-derived growth factor induced the tyrosine...

Topics

3T3 Cells
Adaptor Proteins, Signal Transducing
Adipocytes
Amino Acid Sequence
Animals
CHO Cells
Catalysis
Cricetinae
GRB2 Adaptor Protein
Humans
Insulin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Intracellular Signaling Peptides and Proteins

Kinetics

Mice

Molecular Sequence Data

Mutation

Oncogene Proteins

Phosphoproteins

Source

Open in PubMed

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PMID: 7629070
DOI: 10.1074/jbc.270.30.17716

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7629070-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Identification of the major SHPTP2-binding protein that is tyrosine-phosphorylated in response to insulin.PMID 7629070Read ↗

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