c-Cbl Acts as an E3 Ligase Against DDA3 for Spindle Dynamics and Centriole Duplication during Mitosis
- Authors
- Gwon, Dasom; Hong, Jihee; Jang, Chang-Young
- Issue Date
- Dec-2019
- Publisher
- KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
- Keywords
- c-Cbl; centriole; centrosome; DDA3; E3 ligase; spindle dynamics
- Citation
- MOLECULES AND CELLS, v.42, no.12, pp 840 - 849
- Pages
- 10
- Journal Title
- MOLECULES AND CELLS
- Volume
- 42
- Number
- 12
- Start Page
- 840
- End Page
- 849
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/2687
- DOI
- 10.14348/molcells.2019.0142
- ISSN
- 1016-8478
0219-1032
- 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.
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