Modulation of GaIT1 and SiaIT1 sub-Golgi localization by SiaIT2 expression reveals an organellar level of glycolipid synthesis control.

ULIANA A.S.; CRESPO P.M.; MARTINA J.A.; DANIOTTI J.L.; MACCIONI H.J.F.

JOURNAL OF BIOLOGICAL CHEMISTRY

American Society for Biochemistry and Molecular Biology

Lugar: Bethesda; Año: 2006 vol. 281 p. 32852 - 32852

0021-9258

font face="WarnockPro-Semibold" size="2"> Ganglioside glycosyltransferases organize as multienzyme complexes that localize in different sub-Golgi compartments. Here we studied whether in CHO-K1 cells lacking CMP-NeuAc:GM3sialyltransferase (SialT2), the sub-Golgi localization of UDPGal:glucosylceramide -1,4-galactosyltransferase (GalT1) and CMP-NeuAc:lactosylceramide sialyltransferase (SialT1) complex affected when SialT2, another member of this complex, is coexpressed. GalT1 and SialT1 sub-Golgi localization was determined by studying the effect of brefeldin A (BFA) and monensin on the synthesis of glycolipids and on the sub-Golgi localization of GalT11–52-CFP (cyan fluorescent protein) and SialT11–54