Neural Wiskott Aldrich Syndrome Protein (N-WASP) and the Arp 2/3 complex are recruited to sites of clathrin-mediated endocytosis in cultured fibroblasts

Christien J. Merrifield, Britta Qualmann, Michael M. Kessels, Wolfhard Almers

Research output: Contribution to journalArticlepeer-review

164 Scopus citations

Abstract

Several findings suggest that actin-mediated motility can play a role in clathrin-mediated endocytosis but it remains unclear whether and when key proteins required for this process are recruited to endocytic sites. Here we investigate this question in live Swiss 3T3 cells using two-colour evanescent field (EF) microscopy. We find that Arp3, a component of the Arp2/3 complex, appears transiently while single clathrin-coated pits internalize. There is also additional recruitment of Neural-Wiskott Aldrich Syndrome Protein (N-WASP), a known activator of the Arp2/3 complex. Both proteins appear at about the same time as actin. We suggest that N-WASP and the Arp2/3 complex trigger actin polymerization during a late step in clathrin-mediated endocytosis, and propel clathrin-coated pits or vesicles from the plasma membrane into the cytoplasm.

Original languageEnglish (US)
Pages (from-to)13-18
Number of pages6
JournalEuropean Journal of Cell Biology
Volume83
Issue number1
DOIs
StatePublished - Feb 2004

Keywords

  • Actin mediated mortility
  • Protein interactions in vivo
  • Two colour evanescent field microscopy

ASJC Scopus subject areas

  • Pathology and Forensic Medicine
  • Histology
  • Cell Biology

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