TY - JOUR
T1 - A novel kinase cascade mediated by mitogen-activated protein kinase kinase 6 and MKK3
AU - Moriguchi, Tetsuo
AU - Kuroyanagi, Noriyo
AU - Yamaguchi, Kyoko
AU - Gotoh, Yukiko
AU - Irie, Kenji
AU - Kano, Takahisa
AU - Shirakabe, Kyoko
AU - Muro, Yoshinao
AU - Shibuya, Hiroshi
AU - Matsumoto, Kunihiro
AU - Nishida, Eisuke
AU - Hagiwara, Masatoshi
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 1996
Y1 - 1996
N2 - A cDNA encoding a novel member of the mitogen-activated protein kinase kinase (MAPKK) family, MAPKK6, was isolated and found to encode a protein of 334 amine acids, with a calculated molecular mass of 37 kDa that is 79% identical to MKK3. MAPKK6 was shown to phosphorylate and specifically activate the p38/MPK2 subgroup of the mitogen-activated protein kinase superfamily and could be demonstrated to be phosphorylated and activated in vitro by TAK1, a recently identified MAPKK kinase. MKK3 was also shown to be a good substrate for TAK1 in vitro. Furthermore, when co-expressed with TAK1 in cells in culture, both MAPKK6 and MKK3 were strongly activated. In addition, co-expression of TAK1 and p38/MPK2 in cells resulted in activation of p38/MPK2. These results indicate the existence of a novel kinase cascade consisting of TAK1, MAPKK6/MKK3, and p38/MPK2.
AB - A cDNA encoding a novel member of the mitogen-activated protein kinase kinase (MAPKK) family, MAPKK6, was isolated and found to encode a protein of 334 amine acids, with a calculated molecular mass of 37 kDa that is 79% identical to MKK3. MAPKK6 was shown to phosphorylate and specifically activate the p38/MPK2 subgroup of the mitogen-activated protein kinase superfamily and could be demonstrated to be phosphorylated and activated in vitro by TAK1, a recently identified MAPKK kinase. MKK3 was also shown to be a good substrate for TAK1 in vitro. Furthermore, when co-expressed with TAK1 in cells in culture, both MAPKK6 and MKK3 were strongly activated. In addition, co-expression of TAK1 and p38/MPK2 in cells resulted in activation of p38/MPK2. These results indicate the existence of a novel kinase cascade consisting of TAK1, MAPKK6/MKK3, and p38/MPK2.
UR - http://www.scopus.com/inward/record.url?scp=15844431960&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=15844431960&partnerID=8YFLogxK
U2 - 10.1074/jbc.271.23.13675
DO - 10.1074/jbc.271.23.13675
M3 - Article
C2 - 8663074
AN - SCOPUS:15844431960
VL - 271
SP - 13675
EP - 13679
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 23
ER -