TY - JOUR
T1 - Dimerization in MAP-kinase signaling
AU - Cobb, Melanie H.
AU - Goldsmith, Elizabeth J.
N1 - Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 2000/1/1
Y1 - 2000/1/1
N2 - 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. Copyright (C) 2000 Elsevier Science Ltd.
AB - 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. Copyright (C) 2000 Elsevier Science Ltd.
UR - http://www.scopus.com/inward/record.url?scp=0033983872&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033983872&partnerID=8YFLogxK
U2 - 10.1016/S0968-0004(99)01508-X
DO - 10.1016/S0968-0004(99)01508-X
M3 - Comment/debate
C2 - 10637602
AN - SCOPUS:0033983872
SN - 0968-0004
VL - 25
SP - 7
EP - 9
JO - Trends in biochemical sciences
JF - Trends in biochemical sciences
IS - 1
ER -