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A more recent version of this article appeared on June 1, 2002
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Submitted on December 17, 2001
Revised on February 8, 2002
Accepted on March 8, 2002
1 Laboratory of Morphogenesis and Cell Signaling, UMR144 CNRS, Institut Curie, Paris (present address: Max Planck Institute of Molecular Cell Biology and Genetics, Dresden)
2 Institut Jacques Monod, CNRS, Universite Paris 6-7, France
3 Laboratory of Morphogenesis and Cell Signaling, UMR144 CNRS, Institut Curie, Paris
4 UMR176 CNRS, Institut Curie, Paris, France
* Corresponding author. E-mail address: zahraoui{at}curie.fr.
Junctional complexes such as tight junctions (TJ), and adherens junctions are required for maintaining cell surface asymmetry and polarized transport in epithelial cells. We have shown that Rab13 is recruited to junctional complexes from a cytosolic pool after cell-cell contact formation. In this study, we investigate the role of Rab13 in modulating TJ structure and functions in epithelial MDCK cells. We generate stable MDCK cell lines expressing inactive (T22N mutant) and constitutively active (Q67L mutant) Rab13 as GFP-Rab13 chimeras. Expression of GFP-Rab13Q67L delayed the formation of electrically tight epithelial monolayers as monitored by transepithelial electrical resistance (TER) and induced the leakage of small non-ionic tracers from the apical domain. It also disrupted the TJ fence diffusion barrier. Freeze fracture EM analysis revealed that tight junctional structures did not form a continuous belt but rather a discontinuous series of stranded clusters. Immunofluorescence studies showed that the expression of Rab13Q67L delayed the localization of the TJ transmembrane protein, claudin1, at the cell surface. In contrast, the inactive Rab13T22N mutant did not disrupt TJ functions, TJ strand architecture nor claudin1 localization. Our data revealed that Rab13 plays an important role in regulating both the structure and function of tight junctions.
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