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Rab11-FIP2 regulates differentiable steps in transcytosis.
- Source :
-
American journal of physiology. Cell physiology [Am J Physiol Cell Physiol] 2007 Sep; Vol. 293 (3), pp. C1059-72. Date of Electronic Publication: 2007 Jul 11. - Publication Year :
- 2007
-
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.
- Subjects :
- Animals
Cell Line
Cell Polarity physiology
Dogs
Endosomes metabolism
Epithelial Cells cytology
Genes, Dominant
Green Fluorescent Proteins genetics
Humans
Kidney Tubules cytology
Microscopy, Electron
Microtubules metabolism
Microtubules ultrastructure
Mutagenesis, Site-Directed
Point Mutation
Vesicular Transport Proteins metabolism
rab GTP-Binding Proteins
Carrier Proteins genetics
Carrier Proteins metabolism
Epithelial Cells metabolism
Membrane Proteins genetics
Membrane Proteins metabolism
Protein Transport physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0363-6143
- Volume :
- 293
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- American journal of physiology. Cell physiology
- Publication Type :
- Academic Journal
- Accession number :
- 17626244
- Full Text :
- https://doi.org/10.1152/ajpcell.00078.2007