ArticleiScience2019
Two NEMO-like Ubiquitin-Binding Domains in CEP55 Differently Regulate Cytokinesis.
Article in iScience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Semi-automated Detection of Late Cytokinetic Bridges.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Review
- Biallelic missense CEP55 variants cause prenatal MARCH syndrome.Journal of human genetics · 2025Article
- CEP55 as a prognostic indicator and a predictive marker in oral squamous cell carcinoma.International journal of medical sciences · 2025Article
- Article
- CEP55 Inhibitor: Extensive Computational Approach Defining a New Target of Cell Cycle Machinery Agent.Advanced pharmaceutical bulletin · 2022Article
- Global Proteomics Analysis of Bone Marrow: Establishing Talin-1 and Centrosomal Protein of 55 kDa as Potential Molecular Signatures for Myelodysplastic Syndromes.Frontiers in oncology · 2022Article
- Diagnosing and mitigating method-based avidity artifacts that confound polyubiquitin-binding assays.Biophysical reports · 2021Article
- Loss of Coiled-Coil Protein Cep55 Impairs Neural Stem Cell Abscission and Results in p53-Dependent Apoptosis in Developing Cortex.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CEP55 regulates the final critical step of cell division termed cytokinetic abscission. We report herein that CEP55 contains two NEMO-like ubiquitin-binding domains (UBDs), NOA and ZF, which regulate its function in a different manner. In vitro studies of isolated domains showed that NOA adopts a dimeric coiled-coil structure, whereas ZF is based on a UBZ scaffold. Strikingly, CEP55 knocked-down HeLa cells reconstituted with the full-length CEP55 ubiquitin-binding defective mutants, containing structure-guided mutations either in NOA
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