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Ubiquitin receptor protein UBASH3B : a novel regulator of mitotic progression

Abstract : Mitosis ensures equal segregation of the genome. The major mitotic kinase Aurora B controls fidelity of chromosome segregation by its localization to centromeres and microtubules, which requires CUL3-mediated ubiquitylation. However, it remains unknown how ubiquitylated Aurora B is targeted to mitotic structures. Here, I identify ubiquitin-binding domain (UBD) protein UBASH3B that critically regulates chromosome segregation, acting as ubiquitin receptor for Aurora B. UBASH3B directly binds Aurora B, and this interaction is dependent on CUL3 and on ubiquitin recognition. UBASH3B does not regulate protein levels of Aurora B. Instead, UBASH3B localizes to the mitotic spindle and is both required and sufficient to transfer Aurora B to microtubules. Moreover, redistribution of Aurora B from centromeres to microtubules controls timing and fidelity of chromosome segregation and thereby euploidy of cells. Thus, my findings explain how ubiquitin attachment regulates localization and function of Aurora B, linking receptor-mediated ubiquitin signaling to mitosis.
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Submitted on : Tuesday, January 2, 2018 - 1:26:41 AM
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  • HAL Id : tel-01674175, version 1



Ksenia Krupina. Ubiquitin receptor protein UBASH3B : a novel regulator of mitotic progression. Development Biology. Université de Strasbourg, 2014. English. ⟨NNT : 2014STRAJ075⟩. ⟨tel-01674175⟩



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