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

Jae Hoon Ji, Hyo In Hwang, Hee Jae Lee, Sun Yi Hyun, Hoe Jin Kang, Young Joo Jang

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

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).

Original languageEnglish (US)
Pages (from-to)4299-4305
Number of pages7
JournalFEBS Letters
Volume584
Issue number20
DOIs
StatePublished - 2010
Externally publishedYes

Keywords

  • Mitosis
  • Phosphorylation
  • Polo-like kinase-1
  • Polo-like kinase-1 kinase

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology
  • Biophysics
  • Structural Biology
  • Biochemistry
  • Cell Biology

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