Depletion of IK causes mitotic arrest through aberrant regulation of mitotic kinases and phosphatases
  • Lee, Sunyi
  • Han, Sora
  • Jeong, Ae Lee
  • Park, Jeong Su
  • Yang, Young
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초록

IK is known to inhibit the expression of major histocompatibility complex (MHC) class II antigen, but other cellular functions of IK remain to be uncovered. In this study, IK depletion caused misalignment of chromosomes through an increase in Aurora A and PLK1 phosphorylation, which was mediated by a decrease in PP1 and PP2A activities. On the other hand, the treatment of a dual inhibitor against CDK and Aurora kinases overrode IK depletion-induced mitotic arrest through the activation of phosphatase activity. These findings imply that IK is an essential protein for achieving correct mitotic progress through the regulation of mitotic kinases and phosphatases. Structured summary of protein interactions: CIP2A physically interacts with IK by anti bait coip (View interaction) Aurora A physically interacts with IK by anti tag coimmunoprecipitation (View interaction) IK physically interacts with Aurora A by anti bait coip (1, 2) (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

키워드

Aurora ACDK1IKMitotic arrestProtein phosphataseAURORA-A KINASEPROTEIN PHOSPHATASE-1CHROMOSOME SEGREGATIONCENTROSOME MATURATIONCYTOKINE IKCLASS-IIPHOSPHORYLATIONOVEREXPRESSIONAMPLIFICATIONLOCALIZATION
제목
Depletion of IK causes mitotic arrest through aberrant regulation of mitotic kinases and phosphatases
저자
Lee, SunyiHan, SoraJeong, Ae LeePark, Jeong SuYang, Young
DOI
10.1016/j.febslet.2014.06.046
발행일
2014-08
유형
Article
저널명
FEBS Letters
588
17
페이지
2844 ~ 2850