Rab11-FIP2 regulates differentiable steps in transcytosis.

Ducharme NA, Williams JA, Oztan A, Apodaca G, Lapierre LA, Goldenring JR
Am J Physiol Cell Physiol. 2007 293 (3): C1059-72

PMID: 17626244 · DOI:10.1152/ajpcell.00078.2007

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.

MeSH Terms (19)

Animals Carrier Proteins Cell Line Cell Polarity Dogs Endosomes Epithelial Cells Genes, Dominant Green Fluorescent Proteins Humans Kidney Tubules Membrane Proteins Microscopy, Electron Microtubules Mutagenesis, Site-Directed Point Mutation Protein Transport rab GTP-Binding Proteins Vesicular Transport Proteins

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