TY - JOUR
T1 - Phosphatidic acid formation by phospholipase D is required for transport from the endoplasmic reticulum to the Golgi complex
AU - Bi, Kun
AU - Roth, Michael G.
AU - Ktistakis, Nicholas T.
N1 - Funding Information:
We thank Paul Sternweis and Alex Brown for useful discussions. This work was supported by an NIH grant to M.G.R., and an AHA Texas Affiliate grant to N.T.K.
PY - 1997/5/1
Y1 - 1997/5/1
N2 - Background: Lipid molecules may play a regulatory role in the secretory pathway of mammals and yeast. The lipid hydrolase phospholipase D (PLD) is one candidate for mediating regulation of secretion, based on the location of this enzyme and its requirements for activation. Results: We found that primary alcohols, which block formation of phosphatidic acid (PA) by PLD, inhibited the transport of two different viral glycoproteins from the endoplasmic reticulum to the Golgi complex in Chinese 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 transport imposed by primary alcohols was reversed when PA, in the form of liposomes, was exogenously supplied to the culture medium. Conclusions: We suggest that the earliest site of regulation of membrane transport by PLD is within the intermediate compartment between the endoplasmic reticulum and the Golgi complex.
AB - Background: Lipid molecules may play a regulatory role in the secretory pathway of mammals and yeast. The lipid hydrolase phospholipase D (PLD) is one candidate for mediating regulation of secretion, based on the location of this enzyme and its requirements for activation. Results: We found that primary alcohols, which block formation of phosphatidic acid (PA) by PLD, inhibited the transport of two different viral glycoproteins from the endoplasmic reticulum to the Golgi complex in Chinese 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 transport imposed by primary alcohols was reversed when PA, in the form of liposomes, was exogenously supplied to the culture medium. Conclusions: We suggest that the earliest site of regulation of membrane transport by PLD is within the intermediate compartment between the endoplasmic reticulum and the Golgi complex.
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U2 - 10.1016/S0960-9822(06)00153-9
DO - 10.1016/S0960-9822(06)00153-9
M3 - Article
C2 - 9133344
AN - SCOPUS:0031149834
SN - 0960-9822
VL - 7
SP - 301
EP - 307
JO - Current Biology
JF - Current Biology
IS - 5
ER -