Molecular cloning and characterization of a novel protein kinase with a catalytic domain homologous to mitogen-activated protein kinase kinase kinase
| Autor: | D. Jannuzzi, Henri Lichenstein, Xuhong Sunny Wang, K. Diener, Mark M. Zukowski, Zhengbin Yao, Tse-Hua Tan, D.B. Trollinger |
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| Rok vydání: | 1996 |
| Předmět: |
Mitogen-Activated Protein Kinase 3
Molecular Sequence Data Mitogen-activated protein kinase kinase Protein Serine-Threonine Kinases MAP Kinase Kinase Kinase 5 Biochemistry MAP2K7 Mice Animals Humans ASK1 Tissue Distribution c-Raf Amino Acid Sequence RNA Messenger Cloning Molecular Phosphorylation Molecular Biology Mitogen-Activated Protein Kinase 1 MAP kinase kinase kinase biology Base Sequence Chemistry Cyclin-dependent kinase 2 JNK Mitogen-Activated Protein Kinases Cell Biology MAP Kinase Kinase Kinases Molecular biology Enzyme Activation COS Cells Calcium-Calmodulin-Dependent Protein Kinases biology.protein Cyclin-dependent kinase 9 Mitogen-Activated Protein Kinases |
| Zdroj: | The Journal of biological chemistry. 271(49) |
| ISSN: | 0021-9258 |
| Popis: | Mitogen-activated protein kinase (MAPK) signaling cascades include MAPK or extracellular signal-regulated kinase (ERK), MAPK kinase (MKK or MEK), and MAPK kinase kinase (MAPKKK or MEKK). MAPKK kinase/MEKK phosphorylates and activates its downstream protein kinase, MAPK kinase/MEK, which in turn activates MAPK. We report herein the isolation of a cDNA encoding a novel protein kinase designated MAPKKK5 from a human macrophage library. The nucleotide sequence predicts that MAPKKK5 encodes an open reading frame of 1374 amino acids with all 11 kinase subdomains. The putative catalytic domain of MAPKKK5 shows significant sequence homology to the kinase domains of the MAPKKK/MEKK level protein kinases from mouse MEKK2 and -3, Drosophila melanogaster PK92B, Saccharomyces cerevisiae STE11, and Schizosaccharomyces pombe BYR2. Northern blot analysis showed that MAPKKK5 transcript is abundantly expressed in human heart and pancreas. When transiently expressed in COS and 293 cells, MAPKKK5 markedly activated c-Jun N-terminal kinase or stress-activated protein kinase, but not MAPK/ERK. Furthermore, MAPKKK5 that was immunoprecipitated from transfected 293 cells was able to phosphorylate and activate MKK4 in vitro, suggesting that MAPKKK5 may be an upstream activator of MKK4 in the c-Jun N-terminal kinase pathway. |
| Databáze: | OpenAIRE |
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