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A dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis

Academic Article
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Overview

authors

  • Yarar, D.
  • Waterman-Storer, C. M.
  • Schmid, Sandra

publication date

  • February 2005

journal

  • Molecular Biology of the Cell  Journal

abstract

  • Clathrin-mediated endocytosis in mammalian cells is critical for a variety of cellular processes including nutrient uptake and cell surface receptor down-regulation. Despite the findings that numerous endocytic accessory proteins directly or indirectly regulate actin dynamics and that actin assembly is spatially and temporally coordinated with endocytosis, direct functional evidence for a role of actin during clathrin-coated vesicle formation is lacking. Here, we take parallel biochemical and microscopic approaches to address the contribution of actin polymerization/depolymerization dynamics to clathrin-mediated endocytosis. When measured using live-cell fluorescence microscopy, disruption of the F-actin assembly and disassembly cycle with latrunculin A or jasplakinolide results in near complete cessation of all aspects of clathrin-coated structure (CCS) dynamics. Stage-specific biochemical assays and quantitative fluorescence and electron microscopic analyses establish that F-actin dynamics are required for multiple distinct stages of clathrin-coated vesicle formation, including coated pit formation, constriction, and internalization. In addition, F-actin dynamics are required for observed diverse CCS behaviors, including splitting of CCSs from larger CCSs, merging of CCSs, and lateral mobility on the cell surface. Our results demonstrate a key role for actin during clathrin-mediated endocytosis in mammalian cells.

subject areas

  • 3T3 Cells
  • Actins
  • Animals
  • Bicyclo Compounds, Heterocyclic
  • Clathrin
  • Clathrin-Coated Vesicles
  • Cytoskeleton
  • Depsipeptides
  • Endocytosis
  • Fibroblasts
  • Green Fluorescent Proteins
  • Image Processing, Computer-Assisted
  • Luminescent Proteins
  • Mice
  • Microscopy, Fluorescence
  • Models, Biological
  • Thiazoles
  • Thiazolidines
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Identity

PubMed Central ID

  • PMC545926

International Standard Serial Number (ISSN)

  • 1059-1524

Digital Object Identifier (DOI)

  • 10.1091/mbc.E04-09-0774

PubMed ID

  • 15601897
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Additional Document Info

start page

  • 964

end page

  • 975

volume

  • 16

issue

  • 2

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