Journal
JOURNAL OF CELLULAR BIOCHEMISTRY
Volume 105, Issue 1, Pages 167-175Publisher
WILEY-LISS
DOI: 10.1002/jcb.21809
Keywords
Raf-1; PAK5; ERK; mitochondria; kinase; phosphorylation
Categories
Funding
- American Cancer Society [RSG-01-193-01-TBE]
- NIH [5R01CA116356-02]
- NATIONAL CANCER INSTITUTE [R01CA116356] Funding Source: NIH RePORTER
Ask authors/readers for more resources
Raf-1 is an important effector of Ras mediated signaling and is a critical regulator of the ERK/MAPK pathway. Raf-1 activation is controlled in part by phosphorylation on multiple residues, including an obligate phosphorylation site at serine 338. Previously PAK1 and casein kinase II have been implicated as serine 338 kinases. To identify novel kinases that phosphorylate this site, we tested the ability of group II PAKs(PAKs 4-6) to control serine 338 phosphorylation. We observed that all group II PAKs were efficient serine 338 kinases, although only PAK1 and PAK5 significantly stimulated Raf-1 kinase activity. We also showed that PAK5 forms a tight complex with Raf-1 in the cell, but not A-Raf or B-Raf. Importantly, we also demonstrated that the association of Raf-1 with PAK5 targets a subpopulation of Raf-1 to mitochondria. These data indicate that PAK5 is a potent regulator of Raf-1 activity and may control Raf-1 dependent signaling at mitochondria.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available