A. Horvath et al., CERAMIDE SYNTHESIS ENHANCES TRANSPORT OF GPI-ANCHORED PROTEINS TO THEGOLGI-APPARATUS IN YEAST, EMBO journal, 13(16), 1994, pp. 3687-3695
Inhibition of ceramide synthesis by a fungal metabolite; myriocin, lea
ds to a rapid and specific reduction in the rate of transport of glyco
sylphosphatidylinositol (GPI)-anchored proteins to the Golgi apparatus
without affecting transport of soluble or transmembrane proteins. Inh
ibition of ceramide biosynthesis also quickly blocks remodelling of GP
I anchors to their ceramide-containing, mild base-resistant forms. The
se results suggest that the pool of ceramide is rapidly depleted from
early points of the secretory pathway and that its presence at these l
ocations enhances transport of GPI-anchored proteins specifically. A m
utant that is resistant to myriocin reverses its effect on GPI-anchore
d protein transport without reversing its effects on ceramide synthesi
s and remodelling. Two hypotheses are proposed to explain the role of
ceramide in the transport of GPI-anchored proteins.