Direct Interaction between Rab3b and the Polymeric Immunoglobulin Receptor Controls Ligand-Stimulated Transcytosis in Epithelial Cells

We have examined the role of rab3b in epithelial cells. In MDCK cells, rab3b localizes to vesicular structures containing the polymeric immunoglobulin receptor (pIgR) and located subjacent to the apical surface. We found that GTP-bound rab3b directly interacts with the cytoplasmic domain of pIgR. Bi...

Full description

Saved in:
Bibliographic Details
Published in:Developmental cell 2002-02, Vol.2 (2), p.219-228
Main Authors: van IJzendoorn, Sven C.D., Tuvim, Michael J., Weimbs, Thomas, Dickey, Burton F., Mostov, Keith E.
Format: Article
Language:English
Subjects:
Animals
Cell Line
Cell Polarity
Dimerization
Dogs
Epithelial Cells - cytology
Epithelial Cells - immunology
Epithelial Cells - metabolism
Guanosine Triphosphate - metabolism
Immunoglobulin A - chemistry
Immunoglobulin A - immunology
Immunoglobulin A - metabolism
Ligands
Protein Binding
Protein Structure, Tertiary
Protein Transport
rab3 GTP-Binding Proteins - genetics
rab3 GTP-Binding Proteins - metabolism
Receptors, Polymeric Immunoglobulin - chemistry
Receptors, Polymeric Immunoglobulin - immunology
Receptors, Polymeric Immunoglobulin - metabolism
Signal Transduction
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:We have examined the role of rab3b in epithelial cells. In MDCK cells, rab3b localizes to vesicular structures containing the polymeric immunoglobulin receptor (pIgR) and located subjacent to the apical surface. We found that GTP-bound rab3b directly interacts with the cytoplasmic domain of pIgR. Binding of dIgA to pIgR causes a dissociation of the interaction with rab3b, a process that requires dIgA-mediated signaling, Arg657 in the cytoplasmic domain of pIgR, and possibly GTP hydrolysis by rab3b. Binding of dIgA to pIgR at the basolateral surface stimulates subsequent transcytosis to the apical surface. Overexpression of GTP-locked rab3b inhibits dIgA-stimulated transcytosis. Together, our data demonstrate that a rab protein can bind directly to a specific cargo protein and thereby control its trafficking.
ISSN:1534-5807
1878-1551
DOI:10.1016/S1534-5807(02)00115-6