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A Rab11a-enriched subapical membrane compartment regulates a cytoskeleton-dependent transcytotic pathway in secretory epithelial cells of the lacrimal gland
Author(s) -
Shi Xu,
Maria C. Edman,
Mubashera S. Kothawala,
Guoyong Sun,
Lilian Chiang,
Austin K. Mircheff,
Lixin Zhu,
Curtis T. Okamoto,
Sarah F. HammAlvarez
Publication year - 2011
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.088906
Subject(s) - biology , microbiology and biotechnology , endosome , exocytosis , microtubule , actin , cytoskeleton , secretory vesicle , cytoplasm , intraflagellar transport , compartment (ship) , dynein , polymeric immunoglobulin receptor , lacrimal gland , transcytosis , secretion , receptor , cell , endocytosis , antibody , immunology , flagellum , biochemistry , intracellular , oceanography , gene , geology , medicine , pathology
Despite observations that the lacrimal gland has been identified as the principal source of dimeric immunoglobulin A (dIgA) in tears, the mechanism used by lacrimal gland acinar cells (LGACs) to transcytose dIgA produced by interstitial plasma cells is not well-characterized. This study identifies a transcytotic pathway in LGACs regulated by Rab11a for polymeric immunoglobulin receptor (pIgR) and dIgA. EGFP-tagged Rab11a expressed in primary LGACs labeled a unique membrane compartment of comparable localization to endogenous Rab11a beneath the apical plasma membrane. This compartment was enriched in pIgR and clearly distinct from the regulated secretory pathway. Comparison of dIgA uptake in LGACs expressing wild type and dominant negative EGFP-Rab11a showed that the rapid exocytosis of dIgA was inhibited in acini expressing the dominant-negative protein, which additionally redistributed subapical pIgR. The trafficking of EGFP-Rab11a-enriched vesicles was regulated by microtubule-based and myosin Vb motors at distinct steps. Our data suggest that Rab11a is a crucial regulator of dIgA trafficking in primary acinar secretory epithelial cells and further support a role for microtubules, cytoplasmic dynein, actin filaments and myosin Vb in the maintenance of the Rab11a compartment in this primary secretory epithelial cell.

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