K. Bi et al., PHOSPHATIDIC-ACID FORMATION TOY PHOSPHOLIPASE-D IS REQUIRED FOR TRANSPORT FROM THE ENDOPLASMIC-RETICULUM TO THE GOLGI-COMPLEX, Current biology, 7(5), 1997, pp. 301-307
Background: Lipid molecules may play a regulatory role in the secretor
y pathway of mammals and yeast. The lipid hydrolase phospholipase D (P
LD) is one candidate for mediating regulation of secretion, based on t
he location of this enzyme and its requirements for activation. Result
s: We found that primary alcohols, which block formation of phosphatid
ic acid (PA) by PLD, inhibited the transport of two different viral gl
ycoproteins from the endoplasmic reticulum to the Golgi complex in Chi
nese hamster ovary cells. Corresponding secondary alcohols, which are
much less potent in blocking PA formation, were also less effective in
blocking transport of the glycoproteins. The block in glycoprotein tr
ansport imposed by primary alcohols was reversed when PA, in the form
of liposomes, was exogenously supplied to the culture medium. Conclusi
ons: We suggest that the earliest site of regulation of membrane trans
port by PLD is within the intermediate compartment between the endopla
smic reticulum and the Golgi complex.