Ubiquitin Receptor Protein UBASH3B Drives Aurora B Recruitment to Mitotic Microtubules.

Date publication

janvier 2016

Journal

Developmental cell

Auteurs

Membres identifiés du Cancéropôle Est :
Dr POCH Olivier , Dr RAFFELSBERGER Wolfgang , Dr SUMARA Izabela

Tous les auteurs :
Krupina K, Kleiss C, Metzger T, Fournane S, Schmucker S, Hofmann K, Fischer B, Paul N, Porter IM, Raffelsberger W, Poch O, Swedlow JR, Brino L, Sumara I

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/26766443

Résumé

Mitosis ensures equal segregation of the genome and is controlled by a variety of ubiquitylation signals on substrate proteins. However, it remains unexplored how the versatile ubiquitin code is read out during mitotic progression. Here, we identify the ubiquitin receptor protein UBASH3B as an important regulator of mitosis. UBASH3B interacts with ubiquitylated Aurora B, one of the main kinases regulating chromosome segregation, and controls its subcellular localization but not protein levels. UBASH3B is a limiting factor in this pathway and is sufficient to localize Aurora B to microtubules prior to anaphase. Importantly, targeting Aurora B to microtubules by UBASH3B is necessary for the timing and fidelity of chromosome segregation in human cells. Our findings uncover an important mechanism defining how ubiquitin attachment to a substrate protein is decoded during mitosis.

Mots clés

Anaphase, physiology, Aurora Kinase B, metabolism, Cell Line, Chromosome Segregation, genetics, HeLa Cells, Humans, Kinetochores, metabolism, Microtubules, metabolism, Mitosis, physiology, Phosphorylation, Protein Tyrosine Phosphatases, metabolism, Ubiquitin, metabolism, Ubiquitination, physiology

Référence

Dev. Cell. 2016 Jan;36(1):63-78