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Related Concept Videos

The Spindle Assembly Checkpoint02:19

The Spindle Assembly Checkpoint

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The spindle assembly checkpoint is a molecular surveillance mechanism ensuring the fidelity of chromosome segregation during anaphase. The checkpoint monitors the completion of all the prerequisite steps before chromosome segregation to determine whether the segregation process should proceed or be delayed.
Many proteins function together to control the spindle assembly checkpoint. Mutations affecting these proteins may allow cells to proceed into anaphase prematurely, resulting in the...
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At the transition from prophase to metaphase, there is a reduction in cohesion along the chromosomal arms, resulting in the resolution of sister chromatids. However, residual cohesin connections remain to hold the sister chromatids together until the transition from metaphase to anaphase. The residual connection prevents any premature separation of sister chromatids, blocking the risks of aneuploidy within the daughter cells.
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Microtubules form through the end-to-end polymerization of tubulin heterodimers. Kinetochore microtubules originate from the spindle poles, and their plus-ends connect with the kinetochores on sister-chromatids. Ndc80 protein complexes, present on the kinetochore, form low-affinity links with the plus end of these kinetochore microtubules.
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Most animal cells comprise a pair of centrioles together called a centrosome. The cell duplicates its centrosome and contains two centrosomes side-by-side, which begin to move apart during the prophase. As the centrosomes migrate to two different sides of the cell, microtubules start extending from each centrosome toward the other end. The mitotic spindle is composed of the centrosomes and their emerging microtubules.
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Related Experiment Video

Updated: Apr 17, 2026

Reconstitution of Basic Mitotic Spindles in Spherical Emulsion Droplets
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Solving the centriole disengagement puzzle.

Andrew M Fry

    Nature Cell Biology
    |February 14, 2015
    PubMed
    Summary

    The microcephaly protein Cep215 helps centrioles connect. New findings show Cep215 has two pools that are released by specific protein degradation, allowing centrioles to separate.

    Area of Science:

    • Cell biology
    • Centrosome biology
    • Molecular cell biology

    Background:

    • Cep215 is a microcephaly protein involved in centriole engagement during interphase.
    • Centriole duplication and segregation are critical for cell division and organism development.

    Purpose of the Study:

    • To investigate the distinct roles and regulation of Cep215 pools at the centrosome.
    • To elucidate the molecular mechanisms controlling centriole disengagement.

    Main Methods:

    • Immunofluorescence microscopy to visualize Cep215 localization.
    • Biochemical assays to study protein interactions and degradation.
    • Cell cycle analysis to assess centriole dynamics.

    Main Results:

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  • Two distinct pools of Cep215 were identified at centrosomes: one associated with Cep68 and another with pericentrin.
  • Plk1-mediated degradation of Cep68 releases one pool of Cep215.
  • Separase-mediated cleavage of pericentrin releases the second pool of Cep215.

    • Conclusions:

    • Cep215's dual localization and regulated release are crucial for controlling centriole disengagement.
    • The coordinated action of Plk1 and separase on Cep215-associated proteins governs centriole separation.
    • Understanding Cep215 regulation provides insights into centrosome cycle control and microcephaly pathogenesis.