The Arp2/3 complex has essential roles in vesicle trafficking and transcytosis in the mammalian small intestine.

Journal Article (Journal Article)

The Arp2/3 complex is the only known nucleator of branched F-actin filaments. Work in cultured cells has established a wide array of functions for this complex in controlling cell migration, shape, and adhesion. However, loss of Arp2/3 complex function in tissues has yielded cell type-specific phenotypes. Here we report essential functions of the Arp2/3 complex in the intestinal epithelium. The Arp2/3 complex was dispensable for intestinal development, generation of cortical F-actin, and cell polarity. However, it played essential roles in vesicle trafficking. We found that in the absence of ArpC3, enterocytes had defects in the organization of the endolysosomal system. These defects were physiologically relevant, as transcytosis of IgG was disrupted, lipid absorption was perturbed, and neonatal mice died within days of birth. These data highlight the important roles of the Arp2/3 complex in vesicle trafficking in enterocytes and suggest that defects in cytoplasmic F-actin assembly by the Arp2/3 complex, rather than cortical pools, underlie many of the phenotypes seen in the mutant small intestine.

Full Text

Duke Authors

Cited Authors

  • Zhou, K; Sumigray, KD; Lechler, T

Published Date

  • June 1, 2015

Published In

Volume / Issue

  • 26 / 11

Start / End Page

  • 1995 - 2004

PubMed ID

  • 25833710

Pubmed Central ID

  • PMC4472011

Electronic International Standard Serial Number (EISSN)

  • 1939-4586

Digital Object Identifier (DOI)

  • 10.1091/mbc.E14-10-1481


  • eng

Conference Location

  • United States