Activation of the Jnk signaling pathway by a dual-specificity phosphatase, JSP-1

Shen, Y., Luche, R., Wei, B., Gordon, M. L., Diltz, C. D., Tonks, N. K. (November 2001) Activation of the Jnk signaling pathway by a dual-specificity phosphatase, JSP-1. Proceedings of the National Academy of Sciences of the United States of America, 98 (24). pp. 13613-13618. ISSN 0027-8424

[thumbnail of Tonks_PNAS_2002.pdf]
Preview
PDF
Tonks_PNAS_2002.pdf - Published Version

Download (199kB) | Preview

Abstract

The mitogen-activated protein kinases (MAPKs) are integral to the mechanisms by which cells respond to physiological stimuli, such as growth factors, hormones, and cytokines, and to a wide variety of environmental stresses. The MAPKs, which are stimulated by phosphorylation of a TXY motif in their activation loop, are components of signal transduction cascades in which sequential activation of protein kinases culminates in their activation and their subsequent phosphorylation of various effector proteins that mediate the physiological response. MAPKs are also subject to dephosphorylation and inactivation, both by enzymes that recognize the residues of the TXY motif independently and by dual specificity phosphatases, which dephosphroylate both Tyr and Ser/Thr residues. We report the identification and characterization of a novel dual specificity phosphatase. Contrary to expectation, this broadly expressed enzyme did not inactivate MAPKs in transient cotransfection assays but instead displayed the capacity to function as a selective activator of the MAPK ink, hence the name, Jnk Stimulatory Phosphatase-1 (JSP-1). This study illustrates a new aspect of the regulation of MAPK-dependent signal transduction and raises the possibility that JSP-1 may offer a different perspective to the study of various inflammatory and proliferative disorders associated with dysfunctional ink signaling.

Item Type: Paper
Uncontrolled Keywords: PROTEIN-TYROSINE-PHOSPHATASE JUN NH2-TERMINAL KINASE N-TERMINAL KINASE CRYSTAL-STRUCTURE MAP KINASES PTP-PEST TRANSDUCTION INHIBITION FAMILY
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
organs, tissues, organelles, cell types and functions > cell types and functions > cell functions
organs, tissues, organelles, cell types and functions > cell types and functions > cell functions > cell signaling
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein tyrosine phosphatase
CSHL Authors:
Communities: CSHL labs > Tonks lab
Depositing User: Matt Covey
Date: November 2001
Date Deposited: 18 Dec 2013 19:36
Last Modified: 10 Sep 2019 19:06
PMCID: PMC61089
Related URLs:
URI: https://repository.cshl.edu/id/eprint/29016

Actions (login required)

Administrator's edit/view item Administrator's edit/view item