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Long-patch Base Excision Repair01:02

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Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...

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Single-cell Microfluidic Analysis of Bacillus subtilis
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Bud building by septin patch hole punching.

Fabrice Caudron1, Yves Barral

  • 1Department of Biology, Institute of Biochemistry, ETH Zurich, Schafmattstrasse 18, 8093 Zurich, Switzerland.

Developmental Cell
|August 3, 2013
PubMed
Summary
This summary is machine-generated.

Small GTPase Cdc42 initiates cell polarity in yeast. A new study reveals Cdc42, septins, and exocytosis form a feedback system to maintain this polarity site.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Systems Biology

Background:

  • Small GTPase Cdc42 is crucial for establishing cell polarity in budding yeast.
  • Polarity establishment involves complex regulatory networks.

Purpose of the Study:

  • To investigate the integrated roles of Cdc42, septins, and the exocytosis pathway in polarity site definition and insulation.
  • To elucidate the feedback mechanisms governing yeast cell polarity.

Main Methods:

  • In silico modeling to simulate cellular processes.
  • Experimental cell biology techniques to validate model predictions.

Main Results:

  • Cdc42, septins, and the exocytosis pathway are integrated into a cohesive feedback system.
  • This system effectively defines and insulates the site of polarity on the cell membrane.

Conclusions:

  • The interplay between Cdc42, septins, and exocytosis is essential for robust polarity establishment in yeast.
  • Feedback regulation ensures the precise localization and maintenance of the polarity site.