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Membrane assembly modulates the stability of the meiotic spindle-pole body

Erin M Mathieson1, Cindi Schwartz, Aaron M Neiman

  • 1Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA.

Journal of Cell Science
|July 2, 2010
PubMed

Insights

The meiosis II outer plaque (MOP) complex in yeast spore formation undergoes dynamic changes. Its proteins transition from freely exchanging to stable once new membranes form, indicating a structural rearrangement during vesicle fusion.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Yeast Genetics

Background:

  • Spore formation in Saccharomyces cerevisiae involves de novo assembly of prospore membranes.
  • The meiosis II outer plaque (MOP) complex initiates membrane formation at spindle-pole bodies during meiosis II.

Purpose of the Study:

  • To investigate the dynamic changes of MOP proteins during prospore membrane assembly.
  • To understand the role of MOP protein dynamics in vesicle fusion and membrane formation.

Main Methods:

  • Utilized a fluorescence-recovery assay to monitor protein dynamics.
  • Analyzed the exchange rates of MOP proteins and constitutive spindle-pole body proteins.

Main Results:

  • MOP proteins exhibit high exchange rates with a soluble pool before membrane assembly.
  • MOP proteins become stably integrated into the complex after membrane formation.
  • The MOP component Ady4p's role in complex integrity varies with membrane association.

Conclusions:

  • MOP protein dynamics change significantly during vesicle coalescence and membrane formation.
  • These dynamic shifts suggest an architectural rearrangement of the MOP complex.
  • Ady4p is crucial for MOP integrity, with its function adapting to the stage of membrane development.

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