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Science 26 July 1991:
Vol. 253. no. 5018, pp. 401 - 406
DOI: 10.1126/science.1650499
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Articles

Science, Vol 253, Issue 5018, 401-406
Copyright © 1991 by American Association for the Advancement of Science

articles

Protein tyrosine phosphatases: a diverse family of intracellular and transmembrane enzymes

EH Fischer, H Charbonneau, and NK Tonks

Department of Biochemistry, University of Washington, Seattle 98195.

Protein tyrosine phosphatases (PTPs) represent a diverse family of enzymes that exist as integral membrane and nonreceptor forms. The PTPs, with specific activities in vitro 10 to 1000 times greater than those of the protein tyrosine kinases would be expected to effectively control the amount of phosphotyrosine in the cell. They dephosphorylate tyrosyl residues in vivo and take part in signal transduction and cell cycle regulation. Most of the transmembrane forms, such as the leukocyte common antigen (CD45), contain two conserved intracellular catalytic domains; but their external segments are highly variable. The structural features of the transmembrane forms suggest that these receptor-linked PTPs are capable of transducing external signals; however, the ligands remain unidentified. A hypothesis is proposed explaining how phosphatases might act synergistically with the kinases to elicit a full physiological response, without regard to the state of phosphorylation of the target proteins.


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Positive Effects of SH2 Domain-containing Tyrosine Phosphatase SHP-1 on Epidermal Growth Factor- and Interferon-gamma -stimulated Activation of STAT Transcription Factors in HeLa Cells.
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W. C. Glasgow, R. Hui, A. L. Everhart, S. P. Jayawickreme, J. Angerman-Stewart, B.-B. Han, and T. E. Eling (1997)
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Requirement for Tyrosine Phosphatase during Serotonergic Neuromodulation by Protein Kinase C.
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The Receptor-like Protein-tyrosine Phosphatase DEP-1 Is Constitutively Associated with a 64-kDa Protein Serine/ Threonine Kinase.
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S. Kang, P.-c. Liao, D. A. Gage, and W. J. Esselman (1997)
J. Biol. Chem. 272, 11588-11596
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Interleukin-4 (IL-4) Induces Phosphatidylinositol 3-Kinase (p85) Dephosphorylation. IMPLICATIONS FOR THE ROLE OF SHP-1 IN THE IL-4-INDUCED SIGNALS IN HUMAN B CELLS.
F. Imani, K. J. Rager, B. Catipovic, and D. G. Marsh (1997)
J. Biol. Chem. 272, 7927-7931
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Regulation of Src Homology 2-containing Tyrosine Phosphatase 1during Activation of Human Neutrophils. ROLE OF PROTEIN KINASE C.
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J. Biol. Chem. 272, 875-882
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Epidermal Growth Factor (EGF)-induced Generation of Hydrogen Peroxide. ROLE IN EGF RECEPTOR-MEDIATED TYROSINE PHOSPHORYLATION.
Y. S. Bae, S. W. Kang, M. S. Seo, I. C. Baines, E. Tekle, P. B. Chock, and S. G. Rhee (1997)
J. Biol. Chem. 272, 217-221
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STEP61: A Member of a Family of Brain-Enriched PTPs Is Localized to the Endoplasmic Reticulum.
A. Bult, F. Zhao, R. Dirkx Jr., E. Sharma, E. Lukacsi, M. Solimena, J. R. Naegele, and P. J. Lombroso (1996)
J. Neurosci. 16, 7821-7831
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Identification of the Product of Growth Arrest-specific Gene 6as a Common Ligand for Axl, Sky, and Mer Receptor Tyrosine Kinases.
K. Nagata, K. Ohashi, T. Nakano, H. Arita, C. Zong, H. Hanafusa, and K. Mizuno (1996)
J. Biol. Chem. 271, 30022-30027
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Cysteine Mutations in the MAM Domain Result in Monomeric Meprin and Alter Stability and Activity of the Proteinase.
P. Marchand, M. Volkmann, and J. S. Bond (1996)
J. Biol. Chem. 271, 24236-24241
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The X-ray Crystal Structures of Yersinia Tyrosine Phosphatase with Bound Tungstate and Nitrate. MECHANISTIC IMPLICATIONS.
E. B. Fauman, C. Yuvaniyama, H. L. Schubert, J. A. Stuckey, and M. A. Saper (1996)
J. Biol. Chem. 271, 18780-18788
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An Activated Epidermal Growth Factor Receptor/Lck Chimera Restores Early T Cell Receptor-mediated Calcium Response in a CD45-deficient T Cell Line.
P. Duplay, A. Alcover, C. Fargeas, R. P. Sekaly, and P. E. Branton (1996)
J. Biol. Chem. 271, 17896-17902
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Expression of Dominant Negative Mutant SHPTP2 Attenuates Phosphatidylinositol 3`-Kinase Activity via Modulation of Phosphorylation of Insulin Receptor Substrate-1.
S. Ugi, H. Maegawa, A. Kashiwagi, M. Adachi, J. M. Olefsky, and R. Kikkawa (1996)
J. Biol. Chem. 271, 12595-12602
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Activation of Mitogen-activated Protein Kinase by H(2)O(2).
K. Z. Guyton, Y. Liu, M. Gorospe, Q. Xu, and N. J. Holbrook (1996)
J. Biol. Chem. 271, 4138-4142
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Endogenous Reactive Oxygen Intermediates Activate Tyrosine Kinases in Human Neutrophils.
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J. Biol. Chem. 271, 1455-1461
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The Transmembrane Protein-tyrosine Phosphatase LAR Modulates Signaling by Multiple Receptor Tyrosine Kinases.
D. T. Kulas, B. J. Goldstein, and R. A. Mooney (1996)
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J. Biol. Chem. 270, 22208-22217
   Abstract »    Full Text »    PDF »
Association of SH2 Domain Protein Tyrosine Phosphatases with the Epidermal Growth Factor Receptor in Human Tumor Cells.
S. Tomic, U. Greiser, R. Lammers, A. Kharitonenkov, E. Imyanitov, A. Ullrich, and F.-D. Böhmer (1995)
J. Biol. Chem. 270, 21277-21284
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Osmotic Loading of Neutralizing Antibodies Demonstrates a Role for Protein-tyrosine Phosphatase 1B in Negative Regulation of the Insulin Action Pathway.
F. Ahmad, P.-M. Li, J. Meyerovitch, and B. J. Goldstein (1995)
J. Biol. Chem. 270, 20503-20508
   Abstract »    Full Text »    PDF »
Cloning and Characterization of a Saccharomyces cerevisiae Gene Encoding the Low Molecular Weight Protein-tyrosine Phosphatase.
K. Ostanin, C. Pokalsky, S. Wang, and R. L. Van Etten (1995)
J. Biol. Chem. 270, 18491-18499
   Abstract »    Full Text »    PDF »
Are Protein-tyrosine Phosphatases Specific for Phosphotyrosine?.
Z.-Y. Zhang and Z. Y. Zhang (1995)
J. Biol. Chem. 270, 16052-16055
   Abstract »    Full Text »    PDF »
Homophilic Interactions Mediated by Receptor Tyrosine Phosphatases µ and [IMAGE].
G. C. M. Zondag, G. M. Koningstein, Y.-P. Jiang, J. Sap, W. H. Moolenaar, and M. F. B. G. Gebbink (1995)
J. Biol. Chem. 270, 14247-14250
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Differential Regulation of Protein-tyrosine Phosphatases by Integrin [IMAGE][IMAGE][IMAGE][IMAGE] through Cytoskeletal Reorganization and Tyrosine Phosphorylation in Human Platelets.
Y. E. H. T. and Minoru Okuma and Y. Ezumi (1995)
J. Biol. Chem. 270, 11927-11934
   Abstract »    Full Text »    PDF »
The Receptor-like Protein-tyrosine Phosphatase, RPTP[IMAGE], Is Phosphorylated by Protein Kinase C on Two Serines Close to the Inner Face of the Plasma Membrane.
S. Tracy, P. v. d. Geer, and T. Hunter (1995)
J. Biol. Chem. 270, 10587-10594
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Molecular Characterization of the Human Transmembrane Protein-tyrosine Phosphatase [IMAGE].
R. Pulido, N. X. Krueger, C. Serra-Pagès, H. Saito, and M. Streuli (1995)
J. Biol. Chem. 270, 6722-6728
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Fluorescence Resolution of the Intrinsic Tryptophan Residues of Bovine Protein Tyrosyl Phosphatase.
C. Pokalsky, P. Wick, E. Harms, F. E. Lytle, and R. L. Van Etten (1995)
J. Biol. Chem. 270, 3809-3815
   Abstract »    Full Text »    PDF »
cDNA Cloning and Characterization of a Novel Receptor-type Protein Tyrosine Phosphatase Expressed Predominantly in the Brain.
M. Ogata, M. Sawada, Y. Fujino, and T. Hamaoka (1995)
J. Biol. Chem. 270, 2337-2343
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XCL100, an inducible nuclear MAP kinase phosphatase from Xenopus laevis: its role in MAP kinase inactivation in differentiated cells and its expression during early development.
T Lewis, L. Groom, A. Sneddon, C Smythe, and S. Keyse (1995)
J. Cell Sci. 108, 2885-2896
   Abstract »    PDF »
The Role of Phosphotyrosine Signaling Pathway in Parotid Gland Proliferation and Function.
K.R. Purushotham and M.G. Humphreys-Beher (1995)
Critical Reviews in Oral Biology & Medicine 6, 119-131
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Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins.
J. Darnell Jr, I. Kerr, and G. Stark (1994)
Science 264, 1415-1421
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Signal Transduction Mechanisms in Mesenchymal Cells.
B. S. McAllister, J. D. Walters, and M. S. Olson (1994)
Critical Reviews in Oral Biology & Medicine 5, 291-310
   Abstract »    Full Text »    PDF »
Temporal and spatial regulation of the expression of BAD2, a MAP kinase phosphatase, during seizure, kindling, and long-term potentiation..
Z Qian, M Gilbert, and E R Kandel (1994)
Learn. Mem. 1, 180-188
   Abstract »    PDF »
Kallmann Syndrome: From Genetics to Neurobiology.
E. I. Rugarli and A. Ballabio (1993)
JAMA 270, 2713-2716
   Abstract »    PDF »
Mechanism-based inactivation of prostatic acid phosphatase.
J. Myers and T. Widlanski (1993)
Science 262, 1451-1453
   Abstract »    PDF »
Yin and yang of phosphorylation in cytokine signaling.
Y. Tan (1993)
Science 262, 376-377
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Things start getting sticky for a cell surface enzyme.
F Eijgenraam (1993)
Science 261, 833
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PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase.
P. Rohan, P Davis, C. Moskaluk, M Kearns, H Krutzsch, U Siebenlist, and K Kelly (1993)
Science 259, 1763-1766
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