Rab5 and Rab11 are involved in the trafficking of vinculin in renal papillary collecting duct cells

MARÍA GABRIELA MÁRQUEZ; BRANDAN YAMILA; GUAYTIMA EDITH; FAVALE NICOLAS; LUCILA GISELA PESCIO; NORMA BEATRIZ STERIN-SPEZIALE

Potrero de los Funes- San Luis

Congreso; XLVII REUNIÓN ANUAL DE LA SOCIEDAD ARGENTINA DE INVESTIGACIONES BIOQUÍMICAS Y DE BIOLOGÍA MOLECULAR (SAIB); 2011

SOCIEDAD ARGENTINA DE INVESTIGACIONES BIOQUÍMICAS Y DE BIOLOGÍA MOLECULAR (SAIB)

Focal adhesions (FA) are structures of cell attachment to the extracellular matrix. We have showed that bradykinin (BK) induces a dissipation of vinculin-stained FA, with formation of vinculin and PIP2 containing vesicles. At least a fraction of vinculin was delivered to the recycling endosomal compartment. Now, we isolate the vinculin containing vesicles by immunomagnetic method from cultured papillary collecting duct (CD) cells treated or not with BK (1, 5 and 10 min). We analyzed by confocal microscopy, the colocalization of vinculin with Rab5 which is localized in early endosomes and with Rab11which mediates recycling of endocytic vesicles. Vinculin - Rab5 colocalization was found in control and in BK-treated cells in the marginal and perinuclear cell regions, showing stronger overlapping in control than in 1 min BK-treated-cells. No differences were observed at 5 and 10 min. Vinculin also colocalized with Rab11 in perinuclear region in both control and BK-treated cells showing stronger overlap after 5 and 10 min. In the marginal region overlapping was observed only after 5 and 10 min of BK-treatment. The modulation of these vinculin containing vesicles could be a physiological mechanism to reuse the BK-induced internalized vinculin to be delivered for newly forming FA in CD cells.