Mitogen-Activated Protein Kinase Pathways Mediated by ERK, JNK, and p38 Protein Kinases

Author:

Johnson Gary L.1,Lapadat Razvan1

Affiliation:

1. Department of Pharmacology, University of Colorado Health Sciences Center, Denver, CO 80262, USA.

Abstract

Multicellular organisms have three well-characterized subfamilies of mitogen-activated protein kinases (MAPKs) that control a vast array of physiological processes. These enzymes are regulated by a characteristic phosphorelay system in which a series of three protein kinases phosphorylate and activate one another. The extracellular signal–regulated kinases (ERKs) function in the control of cell division, and inhibitors of these enzymes are being explored as anticancer agents. The c-Jun amino-terminal kinases (JNKs) are critical regulators of transcription, and JNK inhibitors may be effective in control of rheumatoid arthritis. The p38 MAPKs are activated by inflammatory cytokines and environmental stresses and may contribute to diseases like asthma and autoimmunity.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference13 articles.

1. Mitogen-Activated Protein Kinase: Conservation of a Three-Kinase Module From Yeast to Human

2. Insulin-stimulated microtubule-associated protein kinase is phosphorylated on tyrosine and threonine in vivo.

3. G. L. Johnson R. Lapadat ERK Pathway Science's STKE (Connections Map as seen November 2002) ;CMP_10705.

4. ___ JNK Pathway Science's STKE (Connections Map as seen November 2002) ;CMP_10827.

5. ___ p38 Pathway Science's STKE (Connections Map as seen November 2002) ;CMP_10958.

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