A Novel Kinase Cascade Mediated by Mitogen-activated Protein Kinase Kinase 6 and MKK3

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 amino acids, with a calculated molecular mass of 37 kDa that is 79% identical to MKK3. MAPKK6 was shown to phosphorylate and specifically activate t...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1996-06, Vol.271 (23), p.13675-13679
Main Authors: Moriguchi, Tetsuo, Kuroyanagi, Noriyo, Yamaguchi, Kyoko, Gotoh, Yukiko, Irie, Kenji, Kano, Takahisa, Shirakabe, Kyoko, Muro, Yoshinao, Shibuya, Hiroshi, Matsumoto, Kunihiro, Nishida, Eisuke, Hagiwara, Masatoshi
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Autoantibodies - blood
Base Sequence
Behcet Syndrome - enzymology
Behcet Syndrome - immunology
Calcium-Calmodulin-Dependent Protein Kinases - genetics
Calcium-Calmodulin-Dependent Protein Kinases - immunology
Calcium-Calmodulin-Dependent Protein Kinases - metabolism
Cell Line
DNA Probes - genetics
DNA, Complementary - genetics
Enzyme Activation
HeLa Cells
Humans
In Vitro Techniques
MAP Kinase Kinase 3
MAP Kinase Kinase 6
Mitogen-Activated Protein Kinase Kinases
Molecular Sequence Data
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Protein-Tyrosine Kinases - genetics
Protein-Tyrosine Kinases - metabolism
Substrate Specificity
Transfection
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 amino 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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.271.23.13675