INVESTIGADORES
LEIVA Natalia Lorena
congresos y reuniones científicas
Título:
RAB11, RAB14 AND RAB22: THREE SMALL GTPASES JOINEDAT THE ENDOCYTIC / RECYCLING PATHWAY
Autor/es:
CAPMANY A; PAVAROTTI M; LEIVA N; MAGADÁN J; MAYORGA LS; DAMIANI MT
Lugar:
Mar del Plata, Buenos Aires, Argentina
Reunión:
Congreso; XLIII Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular.; 2007
Institución organizadora:
Sociedad Argentina de Investigaciones en Bioquímica y Biología Molecular.
Resumen:
Rabs GTPases regulate intracellular trafficking and maintain
structural identity by overseeing the vectorial transport of proteins
and membranes between organelles. Rab proteins function as
molecular switches by cycling between inactive GDP and active
GTP bound forms. Each Rab protein controls a specific membrane
transport step. Rab11 is present at the endocytic recycling
compartment and TGN derived vesicles. Rab14 is localized at the
Golgi/TGN and early endosomes. Rab22 is associated to
early/sorting endosomes. As these Rabs share similar intracellular
distribution, our goal was to analyze the degree of overlapping
vesicular localization and function. These Rab proteins and some
mutant forms were over-expressed fused to different fluorescent
tags to assess their intracellular localization by confocal
microscopy. Rab11wt and Rab14 wt almost completely colocalized
at the endocytic recycling compartment and TGN
vesicles. Rab14 wt and Rab22 wt were present in the same vesicles
at the perinuclear region and also co-localized in some peripheral
endosomes. The Rab14 GDP-bound form (Rab14S25N) and a
truncated that does not associate to membranes (Rab14 GCGC)
did not co-localize with Rab22wt.The results using mutants and
different expression levels indicate that these proteins influence the
localization of the each other and that they are present at the same
domains on the membrane vesicle. These Rabs acting coordinately
would control molecular trafficking between endocytic/biosynthetic
pathways.