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Vol. 13, Issue 6, 1819-1831, June 2002
*Laboratory of Morphogenesis and Cell Signaling, UMR144 Centre
National de la Recherche Scientifique (CNRS), Institut Curie, Paris;
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 nonionic 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.
Institut Jacques Monod, CNRS, Universite Paris 6-7,
Paris; and §UMR176 CNRS, Institut Curie, Paris, France
Corresponding author. E-mail address:
zahraoui{at}curie.fr.
Present address: Max Planck Institute of Molecular
Cell Biology and Genetics, Dresden, Germany.
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