TY - JOUR
T1 - Cell condition-dependent regulation of ERK5 by cAMP
AU - Pearson, Gray W.
AU - Cobb, Melanie H.
PY - 2002/12/13
Y1 - 2002/12/13
N2 - ERK5 activity is increased by agents known to activate receptor tyrosine kinases, G-protein coupled receptors, and stress response pathways. We now find a role for cAMP in the regulation of ERK5. ERK5 is activated by forskolin, isoproterenol, and epinephrine in NIH3T3 cells and C2C12 myoblasts. ERK1/2 are also activated by cAMP in NIH3T3 cells, but not in C2C12 myoblasts, demonstrating differential regulation of ERK5 and ERK1/2 by cAMP. We examined the effect of cell context on ac. tivation of ERK5 and discovered ERK5 activity is inhibited, rather than activated, by cAMP in confluent, serum-deprived NIH3TS cells and C2C12 myoblasts. Our results suggest that regulation of MAP kinase pathways by cAMP CAMP is not only dictated by cell type, but also by cell context.
AB - ERK5 activity is increased by agents known to activate receptor tyrosine kinases, G-protein coupled receptors, and stress response pathways. We now find a role for cAMP in the regulation of ERK5. ERK5 is activated by forskolin, isoproterenol, and epinephrine in NIH3T3 cells and C2C12 myoblasts. ERK1/2 are also activated by cAMP in NIH3T3 cells, but not in C2C12 myoblasts, demonstrating differential regulation of ERK5 and ERK1/2 by cAMP. We examined the effect of cell context on ac. tivation of ERK5 and discovered ERK5 activity is inhibited, rather than activated, by cAMP in confluent, serum-deprived NIH3TS cells and C2C12 myoblasts. Our results suggest that regulation of MAP kinase pathways by cAMP CAMP is not only dictated by cell type, but also by cell context.
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U2 - 10.1074/jbc.M208535200
DO - 10.1074/jbc.M208535200
M3 - Article
C2 - 12297510
AN - SCOPUS:0037073764
SN - 0021-9258
VL - 277
SP - 48094
EP - 48098
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 50
ER -