Format

Send to

Choose Destination
Cell Cycle. 2013 Mar 15;12(6):1000-8. doi: 10.4161/cc.23947. Epub 2013 Feb 26.

Dma/RNF8 proteins are evolutionarily conserved E3 ubiquitin ligases that target septins.

Author information

1
The Gurdon Institute, University of Cambridge, Cambridge, UK.

Abstract

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 SEPT7, 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.

KEYWORDS:

Chfr; Dma1; Dma2; E3 ubiquitin ligase; RNF8; cytokinesis; midbody; septin-ring; septins; ubiquitin

PMID:
23442799
PMCID:
PMC3637335
DOI:
10.4161/cc.23947
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Taylor & Francis Icon for PubMed Central
Loading ...
Support Center