Mol. Cells  https://doi.org/10.14348/molcells.2019.0142
c-Cbl Acts as an E3 Ligase Against DDA3 for Spindle Dynamics and Centriole Duplication during Mitosis
Dasom Gwon1,2, Jihee Hong1,2, and Chang-Young Jang1,*
1Drug Information Research Institute, College of Pharmacy, Sookmyung Women’s University, Seoul 04310, Korea, 2These authors contributed equally to this work.
cyjang@sookmyung.ac.kr
Received June 28, 2019; Revised September 25, 2019; Accepted September 30, 2019.; Published online November 14, 2019.
© Korean Society for Molecular and Cellular Biology. All rights reserved.

ABSTRACT
The spatiotemporal mitotic processes are controlled qualitatively by phosphorylation and qualitatively by ubiquitination. Although the SKP1-CUL1-F-box protein (SCF) complex and the anaphase-promoting complex/cyclosome (APC/C) mainly mediate ubiquitin-dependent proteolysis of mitotic regulators, the E3 ligase for a large portion of mitotic proteins has yet to be identified. Here, we report c-Cbl as an E3 ligase that degrades DDA3, a protein involved in spindle dynamics. Depletion of c-Cbl led to increased DDA3 protein levels, resulting in increased recruitment of Kif2a to the mitotic spindle, a concomitant reduction in spindle formation, and chromosome alignment defects. Furthermore, c-Cbl depletion induced centrosome over-duplication and centriole amplification. Therefore, we concluded that c-Cbl controls spindle dynamics and centriole duplication through its E3 ligase activity against DDA3.
Keywords: c-Cbl, centriole, centrosome, DDA3, E3 ligase, spindle dynamics

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30 November 2019 Volume 42,
Number 11, pp. 739~819

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