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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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Calmodulin Promotes N-BAR Domain-Mediated Membrane Constriction and Endocytosis.

Margaret D Myers1, Sergey Ryazantsev1, Linda Hicke2

  • 1Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA.

Developmental Cell
|April 20, 2016
PubMed
Summary

Calmodulin regulates membrane remodeling proteins like Bin, Amphiphysin, RVS (BAR) domains, crucial for endocytosis. This interaction enhances membrane sculpting, revealing a conserved mechanism for controlling cellular processes.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Membrane remodeling by BAR domain proteins is essential for endocytosis.
  • Regulation of endocytic BAR domain activity remains poorly understood.

Purpose of the Study:

  • To investigate the interaction between yeast Rvs167 N-BAR domain and calmodulin.
  • To elucidate the role of calmodulin in regulating BAR domain-mediated membrane remodeling.

Main Methods:

  • Identified interaction between Rvs167 N-BAR domain and calmodulin.
  • Created calmodulin-binding mutants of Rvs167.
  • Performed in vitro membrane tubulation and constriction assays.
  • Co-expressed calmodulin with mammalian N-BAR domain proteins in vivo.

Main Results:

  • Calmodulin-binding mutants of Rvs167 showed defects in endocytic vesicle release.
  • Calmodulin enhanced membrane tubulation and constriction by wild-type Rvs167 in vitro.
  • Calmodulin bound a subset of mammalian N-BAR domains.
  • Co-expression of calmodulin with endophilin A2 increased membrane tubulation in vivo.

Conclusions:

  • Calmodulin interacts with and regulates the membrane-sculpting activity of endocytic N-BAR domains.
  • This regulation is conserved across species, from yeast to mammals.
  • Calmodulin plays a crucial role in controlling BAR domain function during endocytosis.