Experimental Cell Research 253, 255â270 (1999) Article ID excr.1999.4687, available online at http://www.idealibrary.com on Jessie English,* Gray Pearson,â Julie Wilsbacher,â Jennifer Swantek,â Mahesh Karandikar,â Shuichan Xu,â¡ and Melanie H. Cobbâ ,1 â Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75235-9041; *Department of Biological ResearchâOncology, ScheringâPlough Corporation, Kenilworth, New Jersey 07033; and â¡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 [1â3]. 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 ï¬rst 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
Experimental Cell Research – Elsevier
Published: Nov 25, 1999
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