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Science 19 March 1993:
Vol. 259. no. 5102, pp. 1763 - 1766
DOI: 10.1126/science.7681221
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Articles

Science, Vol 259, Issue 5102, 1763-1766
Copyright © 1993 by American Association for the Advancement of Science

articles

PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase

PJ Rohan, P Davis, CA Moskaluk, M Kearns, H Krutzsch, U Siebenlist, and K Kelly

Laboratory of Pathology, National Cancer Institute, NIH, Bethesda, MD 20892.

Tyrosine phosphorylation of proteins is required for signal transduction in cells and for growth regulation. A mitogen-induced gene (PAC-1) has been cloned from human T cells and encodes a 32-kilodalton protein that contains a sequence that defines the enzymatic site of known protein phosphotyrosine phosphatases (PTPases). Other than this sequence, PAC-1 is different from several other known related PTPases exemplified by PTP-1b. PAC-1 is similar to a phosphatase induced by mitogens or heat shock in fibroblasts, a yeast gene, and a vaccinia virus-encoded serine-tyrosine phosphatase (VH1). PAC-1 was predominantly expressed in hematopoietic tissues and localized to the nucleus in transfected COS-7 cells and in mitogen-stimulated T cells.


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J. Cell Sci. 108, 2885-2896
   Abstract »    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 »
A Novel Cytosolic Dual Specificity Phosphatase, Interacting with Glucokinase, Increases Glucose Phosphorylation Rate.
M. J. Munoz-Alonso, G. Guillemain, N. Kassis, J. Girard, A.-F. Burnol, and A. Leturque (2000)
J. Biol. Chem. 275, 32406-32412
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Substrate Recognition Domains within Extracellular Signal-regulated Kinase Mediate Binding and Catalytic Activation of Mitogen-activated Protein Kinase Phosphatase-3.
A. Nichols, M. Camps, C. Gillieron, C. Chabert, A. Brunet, J. Wilsbacher, M. Cobb, J. Pouyssegur, J. P. Shaw, and S. Arkinstall (2000)
J. Biol. Chem. 275, 24613-24621
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T. R. Johnson, J. R. Biggs, S. E. Winbourn, and A. S. Kraft (2000)
J. Biol. Chem. 275, 31755-31762
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Distinct Binding Determinants for ERK2/p38alpha and JNK MAP Kinases Mediate Catalytic Activation and Substrate Selectivity of MAP Kinase Phosphatase-1.
D. N. Slack, O.-M. Seternes, M. Gabrielsen, and S. M. Keyse (2001)
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Molecular Cloning and Characterization of a Novel Dual Specificity Phosphatase, LMW-DSP2, That Lacks the Cdc25 Homology Domain.
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Novel NEMO/Ikappa B Kinase and NF-kappa B Target Genes at the Pre-B to Immature B Cell Transition.
J. Li, G. W. Peet, D. Balzarano, X. Li, P. Massa, R. W. Barton, and K. B. Marcu (2001)
J. Biol. Chem. 276, 18579-18590
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Endothelin-1 Induces Serine Phosphorylation of the Adaptor Protein p66Shc and Its Association with 14-3-3 Protein in Glomerular Mesangial Cells.
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Discordance between the Binding Affinity of Mitogen-activated Protein Kinase Subfamily Members for MAP Kinase Phosphatase-2 and Their Ability to Activate the Phosphatase Catalytically.
P. Chen, D. Hutter, X. Yang, M. Gorospe, R. J. Davis, and Y. Liu (2001)
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12-O-Tetradecanoylphorbol-13-acetate (TPA)-induced c-Jun N-terminal Kinase (JNK) Phosphatase Renders Immortalized or Transformed Epithelial Cells Refractory to TPA-inducible JNK Activity.
H. Zhou, A. Lin, Z. Gu, S. Chen, N.-H. Park, and R. Chiu (2000)
J. Biol. Chem. 275, 22868-22875
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Activation of p42 Mitogen-activated Protein Kinase (MAPK), but not c-Jun NH2-Terminal Kinase, Induces Phosphorylation and Stabilization of MAPK Phosphatase XCL100 in Xenopus Oocytes.
M. L. Sohaskey and J. E. Ferrell Jr. (2002)
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