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Science 12 March 1993:
Vol. 259. no. 5101, pp. 1611 - 1614
DOI: 10.1126/science.7681217
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Articles

Science, Vol 259, Issue 5101, 1611-1614
Copyright © 1993 by American Association for the Advancement of Science

articles

Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation

W Vogel, R Lammers, J Huang, and A Ullrich

Department of Molecular Biology, Max-Planck-Institut fur Biochemie, Martinsried, Germany.

Regulation of cell proliferation, differentiation, and metabolic homeostasis is associated with the phosphorylation and dephosphorylation of specific tyrosine residues of key regulatory proteins. The phosphotyrosine phosphatase 1D (PTP 1D) contains two amino terminally located Src homology 2 (SH2) domains and is similar to the Drosophila corkscrew gene product, which positively regulates the torso tyrosine kinase signal transduction pathway. PTP activity was found to be regulated by physical interaction with a protein tyrosine kinase. PTP 1D did not dephosphorylate receptor tyrosine kinases, despite the fact that it associated with the epidermal growth factor receptor and chimeric receptors containing the extracellular domain of the epidermal growth factor receptor and the cytoplasmic domain of either the HER2-neu, kit-SCF, or platelet-derived growth factor beta (beta PDGF) receptors. PTP 1D was phosphorylated on tyrosine in cells overexpressing the beta PDGF receptor kinase and this tyrosine phosphorylation correlated with an enhancement of its catalytic activity. Thus, protein tyrosine kinases and phosphatases do not simply oppose each other's action; rather, they may work in concert to maintain a fine balance of effector activation needed for the regulation of cell growth and differentiation.


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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 Molecular Interaction of Fas and FAP-1. A TRIPEPTIDE BLOCKER OF HUMAN Fas INTERACTION WITH FAP-1 PROMOTES Fas-INDUCED APOPTOSIS.
J. Yanagisawa, M. Takahashi, H. Kanki, H. Yano-Yanagisawa, T. Tazunoki, E. Sawa, T. Nishitoba, M. Kamishohara, E. Kobayashi, S. Kataoka, et al. (1997)
J. Biol. Chem. 272, 8539-8545
   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 »
Both SH2 Domains Are Involved in Interaction of SHP-1 with the Epidermal Growth Factor Receptor but Cannot Confer Receptor-directed Activity to SHP-1/SHP-2 Chimera.
T. Tenev, H. Keilhack, S. Tomic, B. Stoyanov, M. Stein-Gerlach, R. Lammers, A. V. Krivtsov, A. Ullrich, and F.-D. Bohmer (1997)
J. Biol. Chem. 272, 5966-5973
   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 »
Erythropoietin Activates Raf1 by an Shc-Independent Pathway in CTLL-EPO-R Cells.
D. L. Barber, C. N. Corless, K. Xia, T. M. Roberts, and A. D. D'Andrea (1997)
Blood 89, 55-64
   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 »
The Properties of the Protein Tyrosine Phosphatase PTPMEG.
M. Gu and P. W. Majerus (1996)
J. Biol. Chem. 271, 27751-27759
   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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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 »
Rapid Identification of Phosphopeptide Ligands for SH2 Domains. SCREENING OF PEPTIDE LIBRARIES BY FLUORESCENCE-ACTIVATED BEAD SORTING.
K. Muller, F. O. Gombert, U. Manning, F. Grossmuller, P. Graff, H. Zaegel, J. F. Zuber, F. Freuler, C. Tschopp, and G. Baumann (1996)
J. Biol. Chem. 271, 16500-16505
   Abstract »    Full Text »    PDF »
Association of Human Protein-tyrosine Phosphatase kappa with Members of the Armadillo Family.
M. Fuchs, T. Muller, M. M. Lerch, and A. Ullrich (1996)
J. Biol. Chem. 271, 16712-16719
   Abstract »    Full Text »    PDF »


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