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Related Concept Videos

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As cells progress into mitosis, the nuclear envelope breaks down, and the condensed chromosomes are exposed to the array of bipolar microtubules of the mitotic spindle. The kinetochore, a large, disc-shaped protein complex, is present at the centromere region of the sister chromatids and acts as a binding site for the microtubules.  Usually, the plus-end of a single microtubule is embedded within the kinetochore. However, some kinetochores first establish lateral contact with the side-wall...
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Spindle assembly occurs through three, often coexisting, pathways – the centrosome-mediated pathway, the chromatin-mediated pathway, and the microtubule-mediated pathway – collectively contributing to form a robust spindle apparatus.
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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Microtubules are dynamic structures that undergo continuous assembly and disassembly. They originate from specialized multi-protein complexes known as microtubule organizing centers or MTOCs. Within the MTOC, the point of origin of the microtubule is known as the minus end, while the end radiating outward is the plus end. Microtubules serve two primary functions — the organization of spindle complexes to separate sister chromatids during mitotic or meiotic cell division and the formation...
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During mitosis, chromosome movements occur through the interplay of multiple piconewton level forces. In prometaphase, these forces help in chromosome assembly or congression at the equatorial plane, eventually leading to their alignment at the metaphase plate. The forces acting on the chromosomes are space and time-dependent; therefore, they vary with the position of the chromosomes as the cell progresses through mitosis. 
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Related Experiment Video

Updated: Feb 17, 2026

Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins
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Structural basis for assembly of the CBF3 kinetochore complex.

Vera Leber1, Andrea Nans2, Martin R Singleton3

  • 1Structural Biology of Chromosome Segregation Laboratory, The Francis Crick Institute, London, UK.

The EMBO Journal
|December 8, 2017
PubMed
Summary

Researchers structurally characterized the CBF3 complex, crucial for budding yeast centromere assembly. They revealed how Ctf13 and Skp1 interact via an F-box to initiate CBF3 complex formation, aiding kinetochore assembly.

Keywords:
CBF3F‐box proteincentromerekinetochoresingle‐particle cryo‐EM

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • Centromeres are specialized chromosomal regions essential for kinetochore assembly and microtubule attachment in eukaryotes.
  • Centromeres are characterized by CENP-A nucleosomes, a histone H3 variant.
  • In budding yeast, the CBF3 complex recognizes specific DNA sequences to initiate centromere establishment.

Purpose of the Study:

  • To determine the high-resolution structure of the core CBF3 complex.
  • To elucidate the structural basis of CBF3 complex assembly.
  • To understand the role of Ctf13 and Skp1 in CBF3 complex formation.

Main Methods:

  • Single-particle cryo-electron microscopy (cryo-EM) at 3.6 Å resolution.
  • Biochemical analysis of protein-protein interactions.

Main Results:

  • A 3.6 Å cryo-EM reconstruction of the core CBF3 complex, including Cep3, Ctf13, and Skp1, was obtained.
  • Ctf13 was structurally defined as an F-box protein belonging to the leucine-rich-repeat family.
  • A novel F-box-mediated interaction between Ctf13 and Skp1 was identified as critical for initial CBF3 complex assembly.

Conclusions:

  • The study provides the first structural insights into the core CBF3 complex.
  • The findings reveal a novel mechanism for the assembly of the CBF3 complex mediated by Ctf13-Skp1 interaction.
  • This structural understanding is fundamental for comprehending centromere establishment and kinetochore assembly in budding yeast.