Journal
CELL CYCLE
Volume 12, Issue 6, Pages 1000-1008Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/cc.23947
Keywords
Chfr; cytokinesis; Dma1; Dma2; E3 ubiquitin ligase; midbody; RNF8; septins; septin-ring; ubiquitin
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Funding
- HFSP
- CRUK [C6/A11226]
- European Research Council
- European Community's Seventh Framework Program [HEALTH-F2-2010-259893]
- CRUK
- Wellcome Trust
- Cancer Research UK [11224] Funding Source: researchfish
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The budding yeast proteins Dma1 and Dma2 are members of the unique FHA-RING domain protein family and are linked to mitotic regulation and septin organization by ill-defined mechanisms. We show that Dma2 has ubiquitin ligase activity, and that septins Shs1 and Cdc11 are likely direct in vivo targets. We further propose that human RNF8, rather than Chfr, is the mammalian Dma homolog. As in yeast, RNF8 localizes to the centrosomes and cell division sites and promotes ubiquitylation of the septin SEPT 7, whose depletion increases cell division anomalies. Together, these findings reveal evolutionary and functional conservation of Dma proteins, and suggest that RNF8 maintains genome stability through independent, yet analogous, nuclear and cytoplasmic ubiquitylation activities.
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