Journal
FEBS LETTERS
Volume 584, Issue 20, Pages 4299-4305Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2010.09.025
Keywords
Polo-like kinase-1; Polo-like kinase-1 kinase; Phosphorylation; Mitosis
Funding
- Dankook University
Ask authors/readers for more resources
Polo-like kinase-1 (Plk1) is phosphorylated on Thr210 for activation during mitosis. Here, we investigated the question of which kinase(s) is the specific upstream kinase of mitotic Plk1. Upstream kinases of Plk1 were purified from mitotic cell extracts through column chromatography procedures, and identified by mass spectrometry. Candidates for Plk1 kinase included p21-activated kinase, aurora A, and mammalian Ste20-like kinases. Immunoprecipitates of these proteins from mitotic cell extracts phosphorylated Plk1 on Thr210. Even if the activity of Aurora A was blocked with a specific inhibitor, Plk1 phosphorylation still occurred, suggesting that function of Plk1 could be controlled by these kinases for proper mitotic progression, as well as by Aurora A in very late G2 phase for the beginning of mitosis. Structured abstract: MINT-7996332: PAK1 (uniprotkb:Q13153) physically interacts (MI:0915) with PLK1 (uniprotkb:P53350) by pull down (MI:0096) MINT-7996345: PAK3 (uniprotkb:O75914) physically interacts (MI:0915) with PLK1 (uniprotkb:P53350) by pull down (MI:0096) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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