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Science 12 March 1993:
Vol. 259. no. 5101, pp. 1607 - 1611
DOI: 10.1126/science.8096088
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Articles

Science, Vol 259, Issue 5101, 1607-1611
Copyright © 1993 by American Association for the Advancement of Science

articles

SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases

GS Feng, CC Hui, and T Pawson

Division of Molecular and Developmental Biology, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada.

A mouse phosphotyrosine phosphatase containing two Src homology 2 (SH2) domains, Syp, was identified. Syp bound to autophosphorylated epidermal growth factor (EGF) and platelet-derived growth factor (PDGF) receptors through its SH2 domains and was rapidly phosphorylated on tyrosine in PDGF- and EGF-stimulated cells. Furthermore, Syp was constitutively phosphorylated on tyrosine in cells transformed by v-src. This mammalian phosphatase is most closely related, especially in its SH2 domains, to the corkscrew (csw) gene product of Drosophila, which is required for signal transduction downstream of the Torso receptor tyrosine kinase. The Syp gene is widely expressed throughout embryonic mouse development and in adult tissues. Thus, Syp may function in mammalian embryonic development and as a common target of both receptor and nonreceptor tyrosine kinases.


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J. Cell Biol. 138, 845-860
   Abstract »    Full Text »    PDF »
Src Homology 2 Protein Tyrosine Phosphatase (SHPTP2)/Src Homology 2 Phosphatase 2 (SHP2) Tyrosine Phosphatase Is a Positive Regulator of the Interleukin 5 Receptor Signal Transduction Pathways Leading to the Prolongation of Eosinophil Survival.
K. Pazdrak, T. Adachi, and R. Alam (1997)
J. Exp. Med. 186, 561-568
   Abstract »    Full Text »    PDF »
Interaction of Growth Hormone-activated STATs with SH2-containing Phosphotyrosine Phosphatase SHP-1 and Nuclear JAK2 Tyrosine Kinase.
P. A. Ram and D. J. Waxman (1997)
J. Biol. Chem. 272, 17694-17702
   Abstract »    Full Text »    PDF »
Characterization of a Novel Tyrosine Phosphorylated 100-kDa Protein That Binds to SHP-2 and Phosphatidylinositol 3'-Kinase in Myeloid Cells.
K. Carlberg and L. R. Rohrschneider (1997)
J. Biol. Chem. 272, 15943-15950
   Abstract »    Full Text »    PDF »
SHP1 and SHP2 Protein-tyrosine Phosphatases Associate with beta c after Interleukin-3-induced Receptor Tyrosine Phosphorylation. IDENTIFICATION OF POTENTIAL BINDING SITES AND SUBSTRATES.
H. Bone, U. Dechert, F. Jirik, J. W. Schrader, and M. J. Welham (1997)
J. Biol. Chem. 272, 14470-14476
   Abstract »    Full Text »    PDF »
Angiotensin II Stimulates Tyrosine Phosphorylation and Activation of Insulin Receptor Substrate 1 and Protein-tyrosine Phosphatase 1D in Vascular Smooth Muscle Cells.
M. S. Ali, B. Schieffer, P. Delafontaine, K. E. Bernstein, B. N. Ling, and M. B. Marrero (1997)
J. Biol. Chem. 272, 12373-12379
   Abstract »    Full Text »    PDF »
Interleukin-3 Induces the Association of the Inositol 5-Phosphatase SHIP with SHP2.
L. Liu, J. E. Damen, M. D. Ware, and G. Krystal (1997)
J. Biol. Chem. 272, 10998-11001
   Abstract »    Full Text »    PDF »
The Protein-tyrosine Phosphatase SHP-2 Binds Platelet/Endothelial Cell Adhesion Molecule-1 (PECAM-1) and Forms a Distinct Signaling Complex during Platelet Aggregation. EVIDENCE FOR A MECHANISTIC LINK BETWEEN PECAM-1- AND INTEGRIN-MEDIATED CELLULAR SIGNALING.
D. E. Jackson, C. M. Ward, R. Wang, and P. J. Newman (1997)
J. Biol. Chem. 272, 6986-6993
   Abstract »    Full Text »    PDF »
Protein-tyrosine Phosphatase SHP2 Is Positively Linked to Proteinase-activated Receptor 2-mediated Mitogenic Pathway.
Z. Yu, S. Ahmad, J.-L. Schwartz, D. Banville, and S.-H. Shen (1997)
J. Biol. Chem. 272, 7519-7524
   Abstract »    Full Text »    PDF »
Protein-Tyrosine Phosphatase 1B Complexes with the Insulin Receptor in Vivo and Is Tyrosine-phosphorylated in the Presence of Insulin.
D. Bandyopadhyay, A. Kusari, K. A. Kenner, F. Liu, J. Chernoff, T. A. Gustafson, and J. Kusari (1997)
J. Biol. Chem. 272, 1639-1645
   Abstract »    Full Text »    PDF »
Molecular Characterization of Specific Interactions between SHP-2 Phosphatase and JAK Tyrosine Kinases.
T. Yin, R. Shen, G.-S. Feng, and Y.-C. Yang (1997)
J. Biol. Chem. 272, 1032-1037
   Abstract »    Full Text »    PDF »
Peroxovanadate Induces Tyrosine Phosphorylation of Multiple Signaling Proteins in Mouse Liver and Kidney.
S. J. Ruff, K. Chen, and S. Cohen (1997)
J. Biol. Chem. 272, 1263-1267
   Abstract »    Full Text »    PDF »
Interferon-beta Interrupts Interleukin-6-Dependent Signaling Events in Myeloma Cells.
L. C. Berger and R. G. Hawley (1997)
Blood 89, 261-271
   Abstract »    Full Text »    PDF »
Characterization of a 115-kDa Protein That Binds to SH-PTP2, a Protein-tyrosine Phosphatase with Src Homology 2Domains, in Chinese Hamster Ovary Cells.
T. Noguchi, T. Matozaki, Y. Fujioka, T. Yamao, M. Tsuda, T. Takada, and M. Kasuga (1996)
J. Biol. Chem. 271, 27652-27658
   Abstract »    Full Text »    PDF »
Activation of Protein-tyrosine Phosphatase SH-PTP2 by a Tyrosine-based Activation Motif of a Novel Brain Molecule.
H. Ohnishi, M. Kubota, A. Ohtake, K. Sato, and S.-i. Sano (1996)
J. Biol. Chem. 271, 25569-25574
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Glucose-induced Tyrosine Phosphorylation of p125 in Beta Cells and Pancreatic Islets. A NOVEL PROXIMAL SIGNAL IN INSULIN SECRETION.
R. J. Konrad, R. M. Dean, R. A. Young, P. C. Billings, and B. A. Wolf (1996)
J. Biol. Chem. 271, 24179-24186
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Epidermal Growth Factor Induces Coupling of Protein-tyrosine Phosphatase 1D to GRB2 via the COOH-terminal SH3 Domain of GRB2.
L. Wong and G. R. Johnson (1996)
J. Biol. Chem. 271, 20981-20984
   Abstract »    Full Text »    PDF »
Insulin Signaling in Mice Expressing Reduced Levels of Syp.
JoanneM. Arrandale, A. Gore-Willse, S. Rocks, J.-M. Ren, J. Zhu, A. Davis, JamesN. Livingston, and DanielU. Rabin (1996)
J. Biol. Chem. 271, 21353-21358
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Alternative exon splicing controls a translational switch from activator to repressor isoforms of transcription factor CREB during spermatogenesis.
W. Walker, C Girardet, and J. Habener (1996)
J. Biol. Chem. 271, 20145-20150
   Abstract »    Full Text »    PDF »


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