TY - JOUR
T1 - Seven helix chemoattractant receptors transiently stimulate mitogen-activated protein kinase in Dictyostelium
T2 - Role of heterotrimeric G proteins
AU - Maeda, Mineko
AU - Aubry, Laurence
AU - Insall, Robert
AU - Gaskins, Chris
AU - Devreotes, Peter N.
AU - Firtel, Richard A.
PY - 1996/2/16
Y1 - 1996/2/16
N2 - Mitogen-activated protein (MAP) kinases are involved in controlling a cell's responses to a variety of stimuli and can be activated by both protein tyrosine kinase and G protein-coupled receptors. It was shown previously that Dictyostelium MAP kinase ERK2 is required for normal activation of adenylyl cyclase and erk2 null cells are aggregation-deficient. In this manuscript, we show that the Dictyostelium MAP kinase ERK2 is rapidly and transiently activated in response to the chemoattractant cAMP. This response requires cAMP receptors, but is independent of the coupled Gα2 subunit and the only known Gβ subunit. These data indicate that ligand-mediated receptor activation of adenylyl cyclase requires two receptor-dependent pathways, one of which requires heterotrimeric G proteins, including Gα2 and the only known Gβ subunit, and the second of which requires ERK2. Our results suggest that ERK2 may be activated by a novel receptor-mediated pathway.
AB - Mitogen-activated protein (MAP) kinases are involved in controlling a cell's responses to a variety of stimuli and can be activated by both protein tyrosine kinase and G protein-coupled receptors. It was shown previously that Dictyostelium MAP kinase ERK2 is required for normal activation of adenylyl cyclase and erk2 null cells are aggregation-deficient. In this manuscript, we show that the Dictyostelium MAP kinase ERK2 is rapidly and transiently activated in response to the chemoattractant cAMP. This response requires cAMP receptors, but is independent of the coupled Gα2 subunit and the only known Gβ subunit. These data indicate that ligand-mediated receptor activation of adenylyl cyclase requires two receptor-dependent pathways, one of which requires heterotrimeric G proteins, including Gα2 and the only known Gβ subunit, and the second of which requires ERK2. Our results suggest that ERK2 may be activated by a novel receptor-mediated pathway.
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U2 - 10.1074/jbc.271.7.3351
DO - 10.1074/jbc.271.7.3351
M3 - Article
C2 - 8631932
AN - SCOPUS:0030023040
VL - 271
SP - 3351
EP - 3354
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 7
ER -