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We have previously shown that Rab27 is involved in the control of isoproterenol (IPR)\u2010induced amylase release from rat parotid acinar cells. Although Rab27 is predominantly localized on secretory granules under resting conditions, changes to its intracellular localization after \u03b2\u2010stimulation have never been elucidated. The present study investigated IPR\u2010induced redistribution of Rab27B in the parotid acinar cells, revealing translocation from secretory granules to the subapical region after 5\u2003min of IPR treatment and then diffusion into the cytosol after 30\u2003min of IPR treatment. Dissociation of Rab27B from the apical plasma membrane is probably mediated through the Rab GDP dissociation inhibitor (GDI) in the cytosol extracting GDP\u2010bound Rab protein from membranes, as a dramatic increase in the amount of the Rab27B\u2013GDI complex in the cytosol was observed 30\u2003min after stimulation with IPR. These results indicate that, in parotid acinar cells, Rab27B is translocated, in a time\u2010dependent manner, from secretory granules into the apical plasma membrane as a result of exposure to IPR, and then into the cytosol through binding with the GDI.<\/jats:p>","DOI":"10.1111\/j.1600-0722.2009.00618.x","type":"journal-article","created":{"date-parts":[[2009,5,6]],"date-time":"2009-05-06T16:50:13Z","timestamp":1241628613000},"page":"224-230","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":20,"title":["Redistribution of small GTP\u2010binding protein, Rab27B, in rat parotid acinar cells after stimulation with 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