Rab11-FIP2 regulates differentiable steps in transcytosis.

  • Ducharme N
  • Williams J
  • Oztan A
 et al. 
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Abstract

Transcytosis through the apical recycling system of polarized cells is regulated by Rab11a and a series of Rab11a-interacting proteins. We have identified a point mutant in Rab11 family interacting protein 2 (Rab11-FIP2) that alters the function of Rab11a-containing trafficking systems. Rab11-FIP2(S229A/R413G) or Rab11-FIP2(R413G) cause the formation of a tubular cisternal structure containing Rab11a and decrease the rate of polymeric IgA transcytosis. The R413G mutation does not alter Rab11-FIP interactions with any known binding partners. Overexpression of Rab11-FIP2(S229A/R413G) alters the localization of a subpopulation of the apical membrane protein GP135. In contrast, Rab11-FIP2(129-512) alters the localization of early endosome protein EEA1. The distributions of both Rab11-FIP2(S229A/R413G) and Rab11-FIP2(129-512) were not dependent on the integrity of the microtubule cytoskeleton. The results indicate that Rab11-FIP2 regulates trafficking at multiple points within the apical recycling system of polarized cells.

Author-supplied keywords

  • Animals
  • Carrier Proteins
  • Carrier Proteins: genetics
  • Carrier Proteins: metabolism
  • Cell Line
  • Cell Polarity
  • Cell Polarity: physiology
  • Dogs
  • Endosomes
  • Endosomes: metabolism
  • Epithelial Cells
  • Epithelial Cells: cytology
  • Epithelial Cells: metabolism
  • Genes, Dominant
  • Green Fluorescent Proteins
  • Green Fluorescent Proteins: genetics
  • Humans
  • Kidney Tubules
  • Kidney Tubules: cytology
  • Membrane Proteins
  • Membrane Proteins: genetics
  • Membrane Proteins: metabolism
  • Microscopy, Electron
  • Microtubules
  • Microtubules: metabolism
  • Microtubules: ultrastructure
  • Mutagenesis, Site-Directed
  • Point Mutation
  • Protein Transport
  • Protein Transport: physiology
  • Vesicular Transport Proteins
  • Vesicular Transport Proteins: metabolism

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Authors

  • Nicole a Ducharme

  • Janice a Williams

  • Asli Oztan

  • Gerard Apodaca

  • Lynne a Lapierre

  • James R Goldenring

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