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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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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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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.
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Updated: Nov 10, 2025

Automated Analysis of a Nematode Population-based Chemosensory Preference Assay
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Chaperoning SNARE Folding and Assembly.

Yongli Zhang1, Frederick M Hughson2

  • 1Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520, USA;

Annual Review of Biochemistry
|April 7, 2021
PubMed
Summary
This summary is machine-generated.

Sec1/Munc18 (SM) proteins act as essential chaperones, facilitating the rapid and accurate assembly of SNARE proteins, which are crucial for intracellular membrane fusion and exocytosis. This review highlights recent biochemical and biophysical insights into the SNARE-SM fusion machinery.

Keywords:
Munc18-1SM proteinsSNARE assemblymembrane fusionoptical tweezerstemplate complex

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • SNARE and Sec1/Munc18 (SM) proteins are central to intracellular membrane fusion and exocytosis.
  • The precise physiological pathways of SNARE assembly and the mechanistic roles of SM proteins remain incompletely understood.

Purpose of the Study:

  • To review recent advances in understanding the SNARE-SM fusion machinery, focusing on synaptic vesicle fusion.
  • To elucidate the roles of SM proteins in SNARE assembly and membrane fusion.

Main Methods:

  • Biochemical and biophysical studies of SNARE and SM proteins.
  • In vitro analysis of SNARE folding, assembly, energetics, pathways, and kinetics.
  • Investigation of SM-SNARE interactions and their in vivo impact.

Main Results:

  • SM proteins function as chaperones, essential for enabling fast and accurate SNARE assembly.
  • Evidence supports SM proteins collaborating with other SNARE chaperones like Munc13-1.

Conclusions:

  • SM proteins are critical for efficient SNARE assembly, impacting membrane fusion and exocytosis.
  • Deficiencies in SNARE and SM proteins are implicated in human diseases.