INIMEC - CONICET   05467
INSTITUTO DE INVESTIGACION MEDICA MERCEDES Y MARTIN FERREYRA
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Giardia lamblia and Retromer: two evolutionary ancestors
Autor/es:
MIRAS, SL; RIVERO, MR; FELIZIANI, C; ZAMPONI, N; RÓPOLO, AS; TOUZ, MC
Lugar:
Tucumán. Argentina.
Reunión:
Congreso; XLV Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2009
Institución organizadora:
Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Resumen:
Retromer is an evolutionary conserved protein complex required for endosome-to-Golgi retrieval of lysosomal hydrolases receptors. These complex is compound by five subunits, SNX1 and SNX2 (Sorting Nexins SNX), Vps35, Vps29, and Vps26 (Vps, Vacuolar protein sorting). By searching the GiardiaDB, we found genes that codified to the subcomplex gVps35, gVps29, and gVps26 but not SNX1 or SNX2. Analysis of the sequence and structure of these proteins showed high similarities with the ones described in yeast and mammalian cells. However, because Giardia does not contain a recognized Golgi apparatus or a typical endosome/lysosome system, it is possible that this complex shows many particularities. Over-expression of fusion proteins in transfected cells showed that gVps35 localized around of the nucleus and in the lysosomal-like peripheral vacuoles (PVs), while gVps26 localized mostly in the PVs. Besides, by yeast-two hybrid assays, we found that gVps35 directly binds to gVps29 and the Giardia hydrolase receptor gHR. Disclosing whether or not this complex plays a critical function in protein recycling and cell viability will contribute to understanding how to control the cell cycle and to the understanding of how the endosomal/lysosomal pathway has evolved during the eukaryotic evolution.