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First published online 1 April 2003
doi: 10.1242/jcs.00398
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Research Article |
1 Department of Pharmaceutical Sciences, University of Southern California, 1985
Zonal Avenue, Los Angeles, CA 90033, USA
2 Department of Physiology and Biophysics, University of Southern California,
1985 Zonal Avenue, Los Angeles, CA 90033, USA
3 Department of Ophthalmology, University of Southern California, 1985 Zonal
Avenue, Los Angeles, CA 90033, USA
4 Department of Pathology, University of Southern California, 1985 Zonal Avenue,
Los Angeles, CA 90033, USA
5 Institute for Genetic Medicine, University of Southern California, 1985 Zonal
Avenue, Los Angeles, CA 90033, USA
* Author for correspondence (e-mail: shalvar{at}hsc.usc.edu)
Accepted 28 January 2003
A major function of the acinar cells of the lacrimal gland is the production and stimulated release of tear proteins into ocular surface fluid. We investigate the participation of cytoplasmic dynein in carbachol-stimulated traffic to the apical plasma membrane in primary rabbit lacrimal acinar epithelial cells. Confocal fluorescence microscopy revealed a major carbachol-induced, microtubule-dependent recruitment of cytoplasmic dynein and the dynactin complex into the subapical region. Colocalization studies, sorbitol density gradient/phase partitioning analysis and microtubule-affinity purification of membranes showed that some dynein and dynactin complex were associated with VAMP2-enriched membranes. Adenovirus-mediated overexpression of p50/dynamitin inhibited the recruitment and colocalization of dynein, the dynactin complex and VAMP2 in the subapical region. Nocodazole treatment and p50/dynamitin overexpression also depleted subapical stores of rab3D in resting acini, suggesting that dynein activity was also involved in maintenance of rab3D-enriched secretory vesicles. These data implicate cytoplasmic dynein in stimulated traffic to the apical plasma membrane in these secretory epithelial cells.
Key words: Microtubule, Exocytosis, rab3D, VAMP2, Dynein, Acinar secretion
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