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Am J Physiol Cell Physiol (July 11, 2007). doi:10.1152/ajpcell.00078.2007
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Submitted on February 22, 2007
Accepted on June 22, 2007

RAB11-FIP2 REGULATES DIFFERENTIABLE STEPS IN TRANSCYTOSIS

Nicole A Ducharme1, Janice A Williams, Asli Oztan2, Gerard Apodaca3, Lynne A Lapierre4, and James R Goldenring5*

1 Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, Tennessee, United States
2 Cell Biology & Physiology, University of Pittsburgh, Pittsburgh, Pennsylvania, United States
3 Renal/Electrolyte Division, University of Pittsburgh, Pittsburgh, Pennsylvania, United States
4 Surgery, Vanderbilt University School of Medicine, 37211, Tennessee, United States
5 Surgery, Vanderbilt University School of Medicine, Nashville, Tennessee, United States

* To whom correspondence should be addressed. E-mail: jim.goldenring{at}vanderbilt.edu.

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) which 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 sub-population of the apical membrane protein GP135. In contrast, Rab11-FIP2(129-512) alters the localization of early endosome protein EEA1. The distribution 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.




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[Abstract] [Full Text] [PDF]


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