Diacylglycerol is required for the formation of COPI vesicles in the Golgi-to-ER transport pathway

Diacylglycerol is necessary for trans-Golgi network (TGN) to cell surface transport, but its functional relevance in the early secretory pathway is unclear. Although depletion of diacylglycerol did not affect ER-to-Golgi transport, it led to a redistribution of the KDEL receptor to the Golgi, indica...

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Published in:Molecular biology of the cell 2007-09, Vol.18 (9), p.3250-3263
Main Authors: Fernández-Ulibarri, Inés, Vilella, Montserrat, Lázaro-Diéguez, Francisco, Sarri, Elisabet, Martínez, Susana E, Jiménez, Nuria, Claro, Enrique, Mérida, Isabel, Burger, Koert N J, Egea, Gustavo
Format: Article
Language:English
Subjects:
Animals
Aparell de Golgi
Biological transport
Biological Transport - drug effects
Brefeldin A - pharmacology
Carrier Proteins - metabolism
Cell Membrane - drug effects
Cell Membrane - metabolism
Cercopithecus aethiops
Citologia
Coat Protein Complex I - metabolism
COP-Coated Vesicles - metabolism
COS Cells
Cytology
Diglycerides - metabolism
Diglycerides - pharmacology
Endoplasmic reticulum
Endoplasmic Reticulum - drug effects
Endoplasmic Reticulum - metabolism
Endoplasmic Reticulum - ultrastructure
Estrenes - pharmacology
Golgi apparatus
Golgi Apparatus - drug effects
Golgi Apparatus - metabolism
Golgi Apparatus - ultrastructure
GTPase-Activating Proteins - metabolism
HeLa Cells
Humans
Phorbol 12,13-Dibutyrate - pharmacology
Propranolol - pharmacology
Proteins
Proteïnes
Pyrrolidinones - pharmacology
Rats
Receptors, Peptide - metabolism
Reticle endoplasmàtic
Signal Transduction - drug effects
Transport biològic
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Summary:Diacylglycerol is necessary for trans-Golgi network (TGN) to cell surface transport, but its functional relevance in the early secretory pathway is unclear. Although depletion of diacylglycerol did not affect ER-to-Golgi transport, it led to a redistribution of the KDEL receptor to the Golgi, indicating that Golgi-to-ER transport was perturbed. Electron microscopy revealed an accumulation of COPI-coated membrane profiles close to the Golgi cisternae. Electron tomography showed that the majority of these membrane profiles originate from coated buds, indicating a block in membrane fission. Under these conditions the Golgi-associated pool of ARFGAP1 was reduced, but there was no effect on the binding of coatomer or the membrane fission protein CtBP3/BARS to the Golgi. The addition of 1,2-dioctanoyl-sn-glycerol or the diacylglycerol analogue phorbol 12,13-dibutyrate reversed the effects of endogenous diacylglycerol depletion. Our findings implicate diacylglycerol in the retrograde transport of proteins from Golgi to the ER and suggest that it plays a critical role at a late stage of COPI vesicle formation.
ISSN:1059-1524
1939-4586
DOI:10.1091/mbc.E07-04-0334