INVESTIGADORES
GALIANO Mauricio Raul
congresos y reuniones científicas
Título:
Dynamic association of Rpt5 to cold-stable microtubules in glial cells
Autor/es:
JÉSICA FLORES MARTÍN; BONNET, LAURA V.; PALANDRI ANABELA; HALLAK, MARTA E.; GALIANO, MAURICIO R.
Lugar:
Carlos Paz, Córdoba
Reunión:
Congreso; XXXIV Reunión Anual SAN 2019; 2019
Institución organizadora:
Sociedad Argentina de investigación en Neurociencias
Resumen:
The ubiquitin-proteasome system (UPS) is a key cellular complex devoted to proteostasis maintenance. Alterations of its proteolytic activity are closely linked to pathogenesis of cancer or neurodegenerative disorders. Two main complexes form the 26S proteasome, the regulatory particle 19S proteasome and the central particle 20S proteasome. Different reports showed the impairment of proteasomal activity induced by stress conditions. Our study was aimed to analyze how are affected the UPS in glial cells exposed to cold temperature. As expected, a strong reduction on 20S proteasome activity was determined by enzymatic assay that, together with increased accumulation of poly-ubiquitinated proteins shown by Western blot, indicates a reduction in the activity of the UPS under cold condition. By immunofluorescence we observed a clear redistribution of Rpt5 (subunit of 19S complex) associated to a subpopulation of cold stable microtubules (Mts) but, no apparent changes on cellular distribution of alfa1-7 subunits of 20S was observed in Schwann cells, astrocytes or oligodendrocytes exposed to cold temperature. Biochemical evidences of Rpt5/MAP6/tubulin interactions were obtained from immunoprecipitation assays. We also found that this association of Rpt5 to Mts is reversible and specific of this subunit. Hence, the association of Rpt5 to Mts may correspond to a physiological response to cold temperature, as part of a reduced function of proteasome regulatory particle in glia cells.