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Macromolecular assembly depends on tightly regulated pairwise binding interactions that are selectively favored at assembly sites while being disfavored in the soluble phase. This selective control can arise due to molecular density-enhanced binding, as recently found for the kinetochore scaffold protein CENP-T. When clustered, CENP-T recruits markedly more Ndc80 complexes than its monomeric counterpart, but the underlying molecular basis remains elusive. Here, we use quantitative
A distinctive mechanism of protein-protein interaction underpins the assembly of kinetochores, which is critical for human cell division. During mitosis, the Ndc80 complex must bind tightly to the unstructured N-terminus of its receptor, CENP-T, which is densely clustered at kinetochores. Using single-molecule
- Award ID(s):
- 2029868
- PAR ID:
- 10558195
- Publisher / Repository:
- bioRxiv
- Date Published:
- Format(s):
- Medium: X
- Institution:
- bioRxiv
- Sponsoring Org:
- National Science Foundation
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