ASB7 regulates spindle dynamics and genome integrity by targeting DDA3 for proteasomal degradation.

Keiji Uematsu, Fumihiko Okumura, Syunsuke Tonogai, Akiko Joo-Okumura, Dawit Hailu Alemayehu, Akihiko Nishikimi, Yoshinori Fukui, Kunio Nakatsukasa, Takumi Kamura

The Journal of cell biology 2016 Oct 10

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Proper dynamic regulation of the spindle is essential for successful cell division. However, the molecular mechanisms that regulate spindle dynamics in mitosis are not fully understood. In this study, we show that Cullin 5-interacting suppressor of cytokine signaling box protein ASB7 ubiquitinates DDA3, a regulator of spindle dynamics, thereby targeting it for proteasomal degradation. The presence of microtubules (MTs) prevented the ASB7-DDA3 interaction, thus stabilizing DDA3. Knockdown of ASB7 decreased MT polymerization and increased the proportion of cells with unaligned chromosomes, and this phenotype was rescued by deletion of DDA3. Collectively, these data indicate that ASB7 plays a crucial role in regulating spindle dynamics and genome integrity by controlling the expression of DDA3. © 2016 Uematsu et al.

Citation

Keiji Uematsu, Fumihiko Okumura, Syunsuke Tonogai, Akiko Joo-Okumura, Dawit Hailu Alemayehu, Akihiko Nishikimi, Yoshinori Fukui, Kunio Nakatsukasa, Takumi Kamura. ASB7 regulates spindle dynamics and genome integrity by targeting DDA3 for proteasomal degradation. The Journal of cell biology. 2016 Oct 10;215(1):95-106