IIBBA   05544
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE BUENOS AIRES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
DEPLETION OF BOTH ER GTS CAUSES SEVERE DEFECTS IN C.elegans DEVELOPMENT.
Autor/es:
BUZZI, L ; ARANGO, O; PARODI, A; CASTRO, O.
Lugar:
Villa Carlos Paz, Cordoba, Argentina
Reunión:
Congreso; LIII Annual Meeting of the Argentine Society for Biochemistry and Molecular Biology; 2008
Institución organizadora:
Sociedad Argentina de Bioquímica y Bilogía Molecular
Resumen:
 Quality control mechanisms are in place to ensure that newly synthesized   proteins reach their properly folded conformation. N-glycans contribute to folding efficiency in the ER by a series of oligosaccharide processing and lectin binding reactions. The UDP-glycoprotein glucosyltransferse (GT) functioning  as a conformational sensor is the key element in this  mechanism.  The human genome encodes two GT homologues, HUGT1 and HUGT2, which share 55 % identity, but only HUGT1 is active. C. elegans genome encodes two ER GTs (F48E3.3 and F26H9.8). We examined the consequences of depleting F26H9.8 and F48E3.3 proteins by RNA interference and the results showed that the expression of neither F26H9.8 nor F48E3.3 is essential for viability. However, RNAi against F26H9.8 and F48E3.3 causes morphological and developmental phenotypes and shortened their lifespan. The brood size was decreased and most of the interfered animals showed slow growth, and the development to progressive larval stages was retarded. We observed an impairment of the body movement and about 80% of the F483.3 interfered worms showed either a protruding vulva or had expulsed the intestine, suggesting that the depletion of these proteins causes progressive deterioration of muscle tissue. F48E3.3 RNAi elicits expression of the ER stress marker in SJ4400, suggesting the involvement of F483.3 in ER  quality control.