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Biphasic targeting and cleavage furrow ingression directed by the tail of a myosin II

Xiaodong Fang1, Jianying Luo, Ryuichi Nishihama

  • 1Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.

The Journal of Cell Biology
|December 22, 2010
PubMed

Insights

This study reveals a two-step process for targeting myosin II (Myo1) to the cell division site in yeast. This mechanism guides the actomyosin ring assembly and membrane deposition during cell division.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Cytokinesis relies on the actomyosin ring (AMR) for cell division in eukaryotes.
  • The precise mechanisms of myosin II targeting and AMR assembly, and its coordination with membrane trafficking, are not fully understood.

Purpose of the Study:

  • To elucidate the targeting mechanism of myosin II (Myo1) to the division site in Saccharomyces cerevisiae.
  • To investigate the role of Myo1 in actomyosin ring assembly and its coordination with membrane trafficking during cytokinesis.

Main Methods:

  • Utilized Saccharomyces cerevisiae as a model organism.
  • Investigated protein localization and function through genetic and cell biological approaches.
  • Characterized the role of specific proteins (Bni5, Iqg1) in Myo1 targeting.

Main Results:

  • Identified Myo1 as a two-headed myosin II in yeast.
  • Demonstrated a biphasic targeting mechanism for Myo1, dependent sequentially on Bni5 and Iqg1.
  • Showed that the Myo1 tail can promote the assembly of a functional, albeit
  • headless
  • AMR, guiding membrane deposition and ECM remodeling.

Conclusions:

  • Established a novel biphasic targeting mechanism for myosin II during cell division.
  • Highlighted a role for the actomyosin ring in membrane deposition and extracellular matrix remodeling beyond force generation.
  • Provided new insights into the complex regulation of cytokinesis.

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