Phosphorylation of DEPDC1 at Ser110 is required to maintain centrosome organization during mitosis.

Exp Cell Res

Division of Cancer Biology, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku, Nagoya 466-8550, Japan. Electronic address:

Published: September 2017

AI Article Synopsis

  • DEPDC1 is a protein that is overexpressed in various cancers and plays a key role in cell cycle progression, especially during mitosis.
  • There are two forms of DEPDC1 (isoform a and isoform b), which both increase during mitosis but are degraded after it ends, with DEPDC1a specifically localizing to the centrosome and DEPDC1b to the cell cortex.
  • The study found that DEPDC1a is crucial for maintaining the integrity of the centrosome and organizing the bipolar spindle, with its phosphorylation at Ser110 being essential for its proper localization and function during cell division.

Article Abstract

DEPDC1 (DEP domain containing 1) is overexpressed in multiple cancers and is associated with cell cycle progression. In this report, we have investigated the expression, localization, phosphorylation and function of DEPDC1 during mitosis. DEPDC1 has two isoforms (isoform a and isoform b), and both of them are increased in mitosis and degraded once cells exit mitosis. DEPDC1a is localized to the centrosome in metaphase, whereas DEPDC1b is localized to the entire cell cortex during mitosis. DEPDC1a, but not DEPDC1b, was required for the integrity of centrosome and organization of the bipolar spindle. Mass spectrometry and biochemical analyses revealed phosphorylation of DEPDC1 at Ser110. The phosphorylation of Ser110 is essential for localization of DEPDC1a to the centrosome. Consistently, non-phosphorylation mutants of DEPDC1a did not rescue disruption of centrosome organization by depletion of endogenous DEPDC1. Our results show a novel role for DEPDC1 in maintaining centrosome integrity during mitosis for the accurate distribution of chromosomes.

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Source
http://dx.doi.org/10.1016/j.yexcr.2017.06.005DOI Listing

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