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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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Cep57 regulates human centrosomes through multivalent interactions.

Hung-Wei Yeh1, Po-Pang Chen1, Tzu-Chen Yeh1

  • 1Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 30013, Taiwan.

Proceedings of the National Academy of Sciences of the United States of America
|June 10, 2024
PubMed
Summary
This summary is machine-generated.

Human Cep57 protein controls cell division by organizing the centrosome. Its phase separation, regulated by Cep63, is crucial for microtubule formation and centrosome integrity, with mutations linked to aneuploidy syndrome.

Keywords:
Cep57Cep63centrosomeliquid–liquid phase separationmicrotubule nucleation

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Human Cep57 is a pericentriolar matrix scaffold protein essential for centriole duplication and centrosome maturation.
  • Mutations in Cep57 are linked to mosaic-variegated aneuploidy (MVA) syndrome.
  • Cep57 interacts with Cep63 and Cep152 during interphase, but their molecular interplay is not fully understood.

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying Cep57 function in centrosome organization.
  • To investigate the role of Cep57's distinct domains in its phase separation and microtubule nucleation capabilities.
  • To understand how Cep63 regulates Cep57 activity and how MVA mutations affect Cep57 function.

Main Methods:

  • In vitro characterization of Cep57 liquid-liquid phase separation (LLPS) using purified domains.
  • In vitro microtubule nucleation assays using Cep57 condensates.
  • Cellular experiments involving Cep57 depletion, overexpression of mutants, and analysis of centrosome structure and function.

Main Results:

  • Cep57 undergoes LLPS driven by its NTD, CTD, and LMN domains.
  • Cep57 condensates promote microtubule nucleation in vitro via tubulin concentration mediated by the LMN motif.
  • The LMN motif is essential for centrosomal microtubule aster formation in cells, and Cep63 restricts Cep57 assembly and activity.
  • MVA-associated mutations and overexpression of competitive constructs lead to excessive centrosome duplication, while Cep57 depletion causes PCM disorganization.

Conclusions:

  • Cep57's ability to undergo LLPS is critical for its function as a centrosome scaffold.
  • Multivalent interactions mediated by Cep57, particularly its LMN motif, are essential for accurate microtubule nucleation and centrosome structural integrity.
  • Dysregulation of Cep57 phase separation and interactions contributes to aneuploidy and centrosome duplication defects.