ArticleThe Journal of biological chemistry2013
The Geminin and Idas coiled coils preferentially form a heterodimer that inhibits Geminin function in DNA replication licensing.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- McIdas localizes to centrioles and controls centriole numbers through PLK4-dependent phosphorylation.EMBO reports · 2026Article
- Ependymal and neural stem cells are close relatives.Stem cell reports · 2025Review
- GEMC1 and MCIDAS interactions with SWI/SNF complexes regulate the multiciliated cell-specific transcriptional program.Cell death & disease · 2023Article
- Correlation between DNA Methylation and Cell Proliferation Identifies New Candidate Predictive Markers in Meningioma.Cancers · 2022Article
- Article
- Review
- Controlling centriole numbers: Geminin family members as master regulators of centriole amplification and multiciliogenesis.Chromosoma · 2018Review
- The development and functions of multiciliated epithelia.Nature reviews. Molecular cell biology · 2017Review
- GEMC1 is a critical regulator of multiciliated cell differentiation.The EMBO journal · 2016Article
- GemC1 controls multiciliogenesis in the airway epithelium.EMBO reports · 2016Article
- Mcidas and GemC1/Lynkeas specify embryonic radial glial cells.Neurogenesis (Austin, Tex.) · 2016Article
- The structure of the GemC1 coiled coil and its interaction with the Geminin family of coiled-coil proteins.Acta crystallographica. Section D, Biological crystallography · 2015Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Geminin is an important regulator of proliferation and differentiation in metazoans, which predominantly inhibits the DNA replication licensing factor Cdt1, preventing genome over-replication. We show that Geminin preferentially forms stable coiled-coil heterodimers with its homologue, Idas. In contrast to Idas-Geminin heterodimers, Idas homodimers are thermodynamically unstable and are unlikely to exist as a stable macromolecule under physiological conditions. The crystal structure of the homology regions of Idas in complex with Geminin showed a tight head-to-head heterodimeric coiled-coil. This Idas-Geminin heterodimer binds Cdt1 less strongly than Geminin-Geminin, still with high affinity (∼30 nm), but with notably different thermodynamic properties. Consistently, in Xenopus egg extracts, Idas-Geminin is less active in licensing inhibition compared with a Geminin-Geminin homodimer. In human cultured cells, ectopic expression of Idas leads to limited over-replication, which is counteracted by Geminin co-expression. The properties of the Idas-Geminin complex suggest it as the functional form of Idas and provide a possible mechanism to modulate Geminin activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.