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Depletion of IK causes mitotic arrest through aberrant regulation of mitotic kinases and phosphatases
Author(s) -
Lee Sunyi,
Han Sora,
Jeong Ae Lee,
Park Jeong Su,
Yang Young
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.06.046
Subject(s) - mitosis , kinase , polo like kinase , mitotic exit , microbiology and biotechnology , phosphatase , plk1 , cyclin dependent kinase , biology , phosphorylation , protein phosphatase 2 , biochemistry , cell cycle , spindle apparatus , cell division , cell
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.