ArticleStructure (London, England : 1993)2021
Structural characterization of KKT4, an unconventional microtubule-binding kinetochore protein.
Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Molecular features of myosin F adapted for driving actin flows in Toxoplasma gondii.Journal of cell science · 2026Article
- Aurora B controls anaphase onset and error-free chromosome segregation in trypanosomes.The Journal of cell biology · 2024Article
- NMR study of the structure and dynamics of the BRCT domain from the kinetochore protein KKT4.Biomolecular NMR assignments · 2024Article
- Article
- BRCT Domains: Structure, Functions, and Implications in Disease-New Therapeutic Targets for Innovative Drug Discovery against Infections.Pharmaceutics · 2023Review
- Single-molecule experiments reveal the elbow as an essential folding guide in SMC coiled-coil arms.Biophysical journal · 2022Article
- Divergent polo boxes in KKT2 bind KKT1 to initiate the kinetochore assembly cascade inMolecular biology of the cell · 2022Article
- Plasticity in centromere organization and kinetochore composition: Lessons from diversity.Current opinion in cell biology · 2022Review
- Kinetochore Architecture Employs Diverse Linker Strategies Across Evolution.Frontiers in cell and developmental biology · 2022Review
- Kinetoplastid kinetochore proteins KKT2 and KKT3 have unique centromere localization domains.The Journal of cell biology · 2021Article
- Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The kinetochore is the macromolecular machinery that drives chromosome segregation by interacting with spindle microtubules. Kinetoplastids (such as Trypanosoma brucei), a group of evolutionarily divergent eukaryotes, have a unique set of kinetochore proteins that lack any significant homology to canonical kinetochore components. To date, KKT4 is the only kinetoplastid kinetochore protein that is known to bind microtubules. Here we use X-ray crystallography, NMR spectroscopy, and crosslinking mass spectrometry to characterize the structure and dynamics of KKT4. We show that its microtubule-binding domain consists of a coiled-coil structure followed by a positively charged disordered tail. The structure of the C-terminal BRCT domain of KKT4 reveals that it is likely a phosphorylation-dependent protein-protein interaction domain. The BRCT domain interacts with the N-terminal region of the KKT4 microtubule-binding domain and with a phosphopeptide derived from KKT8. Taken together, these results provide structural insights into the unconventional kinetoplastid kinetochore protein KKT4.
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Registered trials
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