Phosphorylation of CHO1 by Lats1/2 regulates the centrosomal activation of LIMK1 during cytokinesis

Cell Cycle
Ayumi OkamotoHiroshi Nojima

Abstract

Large tumor suppressor 1 and 2 (Lats1/2) regulate centrosomal integrity, chromosome segregation and cytokinesis. As components of the centralspindlin complex, the kinesin-like protein CHO1 and its splicing variant MKLP1 colocalize with chromosome passenger proteins and GTPases and regulate the formation of the contractile ring and cytokinesis; however, the regulatory mechanisms of CHO1/MKLP1 remain elusive. Here, we show that Lats1/2 phosphorylate Ser716 in the F-actin-interacting region of CHO1, which is absent in MKLP1. Phosphorylated CHO1 localized to the centrosomes and midbody, and the actin polymerization factor LIM-kinase 1 (LIMK1) was identified as its binding partner. Overexpression of constitutively phosphorylated and non-phosphorylated CHO1 altered the mitotic localization and activation of LIMK1 at the centrosomes in HeLa cells, leading to the inhibition of cytokinesis through excessive phosphorylation of Cofilin and mislocalization of Ect2. These results suggest that Lats1/2 stringently control cytokinesis by regulating CHO1 phosphorylation and the mitotic activation of LIMK1 on centrosomes.

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Citations

Mar 12, 2016·Seminars in Cell & Developmental Biology·Masanori Mishima
Apr 20, 2019·Proceedings of the National Academy of Sciences of the United States of America·Wantae KimYingzi Yang

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Methods Mentioned

BETA
nucleotide exchange
immunoprecipitation
transfection
PCR
transfections
fluorescence microscopy
electrophoresis

Software Mentioned

ImageJ
Slingshot
Fluoview
MetaView

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