New Insights into the Control of MAP Kinase Pathways

New Insights into the Control of MAP Kinase Pathways Experimental Cell Research 253, 255–270 (1999) Article ID excr.1999.4687, available online at http://www.idealibrary.com on Jessie English,* Gray Pearson,†Julie Wilsbacher,†Jennifer Swantek,†Mahesh Karandikar,†Shuichan Xu,‡ and Melanie H. Cobb†,1 †Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75235-9041; *Department of Biological Research–Oncology, Schering–Plough Corporation, Kenilworth, New Jersey 07033; and ‡Salk Institute, La Jolla, California 92037 INTRODUCTION Mitogen-activated protein (MAP) kinases, found in all eukaryotes, are common participants in signal transduction pathways from the membrane to the nucleus [1–3]. They signal in a wide range of processes from the pheromone control of cell cycle arrest and mating in Saccharomyces cerevisiae, in which these enzymes were first discovered, to proliferation and differentiation in metazoans. These kinases are activated through multistep protein kinase cascades by dual phosphorylation on a tyrosine and a threonine residue. The mammalian MAP kinase family includes ERK1 and ERK2, often referred to as p44 and p42 MAP kinases; 4 isoforms of p38 MAP kinase designated , , (alternative names ERK6 or SAPK3), and ; 3 genes encoding 10 or more splice variants of the c-Jun Nterminal kinase/stress-activated protein kinases (JNK/ SAPKs); at least 3 forms of ERK3 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Experimental Cell Research Elsevier

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Publisher
Elsevier
Copyright
Copyright © 1999 Academic Press
ISSN
0014-4827
D.O.I.
10.1006/excr.1999.4687
Publisher site
See Article on Publisher Site

Abstract

Experimental Cell Research 253, 255–270 (1999) Article ID excr.1999.4687, available online at http://www.idealibrary.com on Jessie English,* Gray Pearson,†Julie Wilsbacher,†Jennifer Swantek,†Mahesh Karandikar,†Shuichan Xu,‡ and Melanie H. Cobb†,1 †Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75235-9041; *Department of Biological Research–Oncology, Schering–Plough Corporation, Kenilworth, New Jersey 07033; and ‡Salk Institute, La Jolla, California 92037 INTRODUCTION Mitogen-activated protein (MAP) kinases, found in all eukaryotes, are common participants in signal transduction pathways from the membrane to the nucleus [1–3]. They signal in a wide range of processes from the pheromone control of cell cycle arrest and mating in Saccharomyces cerevisiae, in which these enzymes were first discovered, to proliferation and differentiation in metazoans. These kinases are activated through multistep protein kinase cascades by dual phosphorylation on a tyrosine and a threonine residue. The mammalian MAP kinase family includes ERK1 and ERK2, often referred to as p44 and p42 MAP kinases; 4 isoforms of p38 MAP kinase designated , , (alternative names ERK6 or SAPK3), and ; 3 genes encoding 10 or more splice variants of the c-Jun Nterminal kinase/stress-activated protein kinases (JNK/ SAPKs); at least 3 forms of ERK3

Journal

Experimental Cell ResearchElsevier

Published: Nov 25, 1999

References

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