ArticleThe Journal of biological chemistry2012
Fission yeast Dma1 requires RING domain dimerization for its ubiquitin ligase activity and mitotic checkpoint function.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- Localization of the ubiquitin ligase Dma1 to the fission yeast contractile ring is modulated by phosphorylation.FEBS letters · 2021Article
- Relief of the Dma1-mediated checkpoint requires Dma1 autoubiquitination and dynamic localization.Molecular biology of the cell · 2018Article
- The RING-Finger Ubiquitin Ligase HAF1 Mediates Heading date 1 Degradation during Photoperiodic Flowering in Rice.The Plant cell · 2015Article
- Feedback regulation of cholesterol uptake by the LXR-IDOL-LDLR axis.Arteriosclerosis, thrombosis, and vascular biology · 2012Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
In fission yeast (Schizosaccharomyces pombe), the E3 ubiquitin ligase Dma1 delays cytokinesis if chromosomes are not properly attached to the mitotic spindle. Dma1 contains a C-terminal RING domain, and we have found that the Dma1 RING domain forms a stable homodimer. Although the RING domain is required for dimerization, residues in the C-terminal tail are also required to help form or stabilize the dimeric structure because mutation of specific residues in this region disrupts Dma1 dimerization. Further analyses showed that Dma1 dimerization is required for proper localization at spindle pole bodies and the cell division site, E3 ligase activity, and mitotic checkpoint function. Thus, Dma1 forms an obligate dimer via its RING domain, which is essential for efficient transfer of ubiquitin to its substrate(s). This study further supports the mechanistic paradigm that many RING E3 ligases function as RING dimers.
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