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Related Concept Videos

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The primary microtubule organizing center (MTOC) in animal cells is the centrosome. A centrosome has two cylindrical centrioles at its core. Each centriole consists of nine sets of three microtubules held together by proteins. The centrioles are positioned at right angles to each other and surrounded by a shapeless protein cloud called the pericentriolar matrix, or pericentriolar material (PCM).
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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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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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Cohesin protein complexes are a molecular glue that holds two sister chromatids together. They play an important role both in mitosis and meiosis. In mitosis, all cohesin complexes present on the chromosomes are removed before the start of the anaphase stage.
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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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Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins
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The A-C linker controls centriole structural integrity and duplication.

Lorène Bournonville1, Marine H Laporte1,2, Susanne Borgers1

  • 1University of Geneva, Faculty of Sciences, Department of Molecular and Cellular Biology, Geneva, Switzerland.

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|July 24, 2025
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Researchers identified new proteins in the centriole

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Microscopy

Background:

  • Centrioles are vital barrel-shaped organelles essential for cell division and ciliogenesis.
  • Specific structural components, like the A-C linker, are critical but poorly understood.
  • The composition of the A-C linker has remained largely unknown.

Purpose of the Study:

  • To characterize the protein composition of the centriole's A-C linker.
  • To investigate the function of A-C linker proteins in centriole structure and duplication.

Main Methods:

  • Ultrastructure expansion microscopy was employed for high-resolution imaging.
  • Protein localization and functional assays were performed.
  • Depletion studies were conducted to assess the roles of identified proteins.

Main Results:

  • CCDC77, WDR67, and MIIP were identified as components of the A-C linker.
  • These proteins form a complex localized between microtubule triplets.
  • Depletion of A-C linker proteins caused microtubule triplet disruption and centriole breakage.
  • The A-C linker and inner scaffold cooperate to maintain centriole architecture.
  • The A-C linker plays a role in centriole duplication via torus regulation.

Conclusions:

  • The A-C linker is composed of CCDC77, WDR67, and MIIP, forming a crucial structural module.
  • This linker complex is essential for maintaining centriole integrity and microtubule cohesion.
  • The A-C linker has an unexpected role in regulating centriole duplication, highlighting its multifaceted functions.