Document Detail

Rab13 mediates the continuous endocytic recycling of occludin to the cell surface.
MedLine Citation:
PMID:  15528189     Owner:  NLM     Status:  MEDLINE    
During epithelial morphogenesis, adherens junctions (AJs) and tight junctions (TJs) undergo dynamic reorganization, whereas epithelial polarity is transiently lost and reestablished. Although ARF6-mediated endocytic recycling of E-cadherin has been characterized and implicated in the rapid remodeling of AJs, the molecular basis for the dynamic rearrangement of TJs remains elusive. Occludin and claudins are integral membrane proteins comprising TJ strands and are thought to be responsible for establishing and maintaining epithelial polarity. Here we investigated the intracellular transport of occludin and claudins to and from the cell surface. Using cell surface biotinylation and immunofluorescence, we found that a pool of occludin was continuously endocytosed and recycled back to the cell surface in both fibroblastic baby hamster kidney cells and epithelial MTD-1A cells. Biochemical endocytosis and recycling assays revealed that a Rab13 dominant active mutant (Rab13 Q67L) inhibited the postendocytic recycling of occludin, but not that of transferrin receptor and polymeric immunoglobulin receptor in MTD-1A cells. Double immunolabelings showed that a fraction of endocytosed occludin was colocalized with Rab13 in MTD-1A cells. These results suggest that Rab13 specifically mediates the continuous endocytic recycling of occludin to the cell surface in both fibroblastic and epithelial cells.
Shinya Morimoto; Noriyuki Nishimura; Tomoya Terai; Shinji Manabe; Yasuyo Yamamoto; Wakako Shinahara; Hidenori Miyake; Seiki Tashiro; Mitsuo Shimada; Takuya Sasaki
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2004-11-04
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  280     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2005 Jan 
Date Detail:
Created Date:  2005-01-17     Completed Date:  2005-04-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2220-8     Citation Subset:  IM    
Department of Biochemistry, Institute of Health Biosciences, The University of Tokushima Graduate School, Tokushima 770-8503, Japan.
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MeSH Terms
Adherens Junctions / metabolism
Biotin / metabolism
Cadherins / metabolism
Cell Line
Endocytosis / physiology*
Membrane Proteins / metabolism*
Microscopy, Fluorescence
Tight Junctions / metabolism
rab GTP-Binding Proteins / physiology*
Reg. No./Substance:
0/Cadherins; 0/Membrane Proteins; 0/occludin; 58-85-5/Biotin; EC 3.6.1.-/RAB13 protein, human; EC 3.6.1.-/rab GTP-Binding Proteins
Erratum In:
J Biol Chem. 2005 Sep 9;280(36):32048

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