Dimerization in MAP-kinase signaling.
The stimulus-dependent nuclear localization of the extracellular-signal- regulated kinases ERK1 and ERK2 is required for many of their actions, including induction of neurites in PC12 cells and transformation of fibroblasts. Phosphorylation of ERK2 causes it to form dimers, and the most flexible portions of the ERK2 molecule provide the surfaces for dimerization. It is thought that dimerization promotes nuclear localization of ERK2 by its effects on import, export or retention in cytoplasmic and nuclear compartments. Dimerization might also influence substrate interactions.
Cobb
M H
MH
Department of Pharmacology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd, Dallas, TX 75235-9041, USA. mcobb@mednet.swmed.edu
Goldsmith
E J
EJ
D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism; D019281:Dimerization; D006801:Humans; D020935:MAP Kinase Signaling System; D019950:Mitogen-Activated Protein Kinase 1 / Q000737:chemistry / Q000378:metabolism; D048052:Mitogen-Activated Protein Kinase 3; D020928:Mitogen-Activated Protein Kinases / Q000737:chemistry* / Q000378:metabolism*; D010766:Phosphorylation; D011487:Protein Conformation; D015398:Signal Transduction
D019950:Mitogen-Activated Protein Kinase 1; D048052:Mitogen-Activated Protein Kinase 3; D020928:Mitogen-Activated Protein Kinases