CONICET | Buscador de Institutos y Recursos Humanos

The investigation of new therapy for neurodegenerative disorders and myopathies lead research efforts to an intensive study of intracellular protein degradation processes. One of the major intracellular protein degradation systems is the autophagy pathway, which is a catabolic process that involves delivery of cellular components to the lysosome for proteolysis. Lysosomes also receive material from the extracellular media via the endosome traffic, which represents the endocytic/lysosomal pathway. Results from our laboratory have demonstrated that Rab24, an atypical Rab protein whose function is currently unknown, is implicated in the autophagy pathway. This protein changes its distribution colocalizing with the autophagosomal markers LC3 and monodansylcadaverine upon autophagy induction. In the present report we have studied the role of Rab24 in the endocytic/lysosomal pathway in K562 cells. We demonstrate that Rab24 colocalizes with markers of the late endocytic/lysosomal compartments (i.e. Rab7 and LAMP1). In addition, the expression of a Rab24 mutant or the silencing of the protein by siRNA, block the lysosomal degradation process. According to our data about Rab24 and Rab7 colocalization and the specific and reciprocal effect in their intracellular distribution, we postulate that these Rabs proteins share regulatory factors, being both Rabs components of the same trafficking pathway.

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