Purification and proteomic identification of putative upstream regulators of polo-like kinase-1 from mitotic cell extracts

被引:9
作者
Ji, Jae-Hoon [1 ]
Hwang, Hyo-In [1 ]
Lee, Hee-Jae [1 ]
Hyun, Sun-Yi [1 ]
Kang, Hoe-Jin [1 ]
Jang, Young-Joo [1 ]
机构
[1] Dankook Univ, Lab Cell Cycle & Signal Transduct, WCU Dept NanoBioMed Sci, Inst Tissue Regenerat Engn ITREN, Cheonan Si 330714, Chungnam, South Korea
关键词
Polo-like kinase-1; Polo-like kinase-1 kinase; Phosphorylation; Mitosis; ANAPHASE-PROMOTING COMPLEX; AURORA-A; PROTEIN-KINASE; SACCHAROMYCES-CEREVISIAE; BOX DOMAIN; PLK; PHOSPHORYLATION; MITOSIS; PLX1; PROGRESSION;
D O I
10.1016/j.febslet.2010.09.025
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:4299 / 4305
页数:7
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