Regulation of a Mitogen-Activated Protein Kinase Kinase Kinase, MLTK by PKN
-
- Takahashi Mikiko
- Biosignal Research Center
-
- Gotoh Yusuke
- Graduate School of Science and Technology, Kobe University
-
- Isagawa Takayuki
- Graduate School of Science and Technology, Kobe University
-
- Nishimura Tamako
- Graduate School of Science and Technology, Kobe University
-
- Goyama Emiko
- Graduate School of Science and Technology, Kobe University
-
- Kim Hon-Song
- Graduate School of Science and Technology, Kobe University
-
- Mukai Hideyuki
- Biosignal Research Center Graduate School of Science and Technology, Kobe University
-
- Ono Yoshitaka
- Biosignal Research Center Graduate School of Science and Technology, Kobe University
Search this article
Abstract
PKNαis a fatty acid- and Rho-activated serine/threonine protein kinase having a catalytic domain homologous to members of the protein kinase C family. Recently it was reported that PKNα is involved in the p38 mitogen-activated protein kinase (MAPK) signaling pathway. To date, however, how PKNα regulates the p38γ MAPK signaling pathway is unclear. Here we demonstrate that PKNα efficiently phosphorylates MLTKαa (MLK-like mitogen-activated protein triple kinase), which was recently identified as a MAPK kinase kinase (MAPKKK) for the p38 MAPK cascade. Phosphorylation of MLTKa by PKNα enhances its kinase activity in vitro. Expression of the kinasenegative mutant of PKNα inhibited the mobility shift of MLTKα caused by osmotic shock in SDS-PAGE. Furthermore, PKNα associates with each member of the p38γ MAPK signaling pathway (p38γ, MKK6, and MLTKα). These results suggest that PKNα functions as not only an upstream activator of MLTKα but also a putative scaffold protein for the p38γ MAPK signaling pathway.
Journal
-
- The Journal of Biochemistry
-
The Journal of Biochemistry 133 (2), 181-187, 2003
The Japanese Biochemical Society
- Tweet
Keywords
Details 詳細情報について
-
- CRID
- 1390282679907970816
-
- NII Article ID
- 130003534501
- 50000765483
-
- NII Book ID
- AA00694073
-
- COI
- 1:CAS:528:DC%2BD3sXjsVamtr4%3D
-
- ISSN
- 17562651
- 0021924X
-
- NDL BIB ID
- 6469590
-
- PubMed
- 12761180
-
- Text Lang
- en
-
- Data Source
-
- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
-
- Abstract License Flag
- Disallowed