PDMP blocks the BFA-induced ADP-ribosylation of BARS-50 in isolated Golgi membranes.
We reported that an inhibitor of sphingolipid biosynthesis, D, L-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol (PDMP), blocks brefeldin A (BFA)-induced retrograde membrane transport from the Golgi complex to the endoplasmic reticulum (ER) (Kok et al., 1998, J. Cell Biol. 142, 25-38). We now show that PDMP partially blocks the BFA-induced ADP-ribosylation of the cytosolic protein BARS-50. Moreover, PDMP does not interfere with the BFA-induced inhibition of the binding of ADP-ribosylation factor (ARF) and the coatomer component beta-coat protein to Golgi membranes. These results are consistent with a role of ADP-ribosylation in the action of BFA and with the involvement of BARS-50 in the regulation of membrane trafficking.
De Matteis
M A
MA
Department of Cell Biology and Oncology, Istituto di Ricerche Farmacologiche Mario Negri, Consorzio Mario Negri Sud, 66030, Sta. Maria Imbaro, Chieti, Italy.
Luna
A
A
Di Tullio
G
G
Corda
D
D
Kok
J W
JW
Luini
A
A
Egea
G
G
D000244:Adenosine Diphosphate / Q000378:metabolism; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D020126:Brefeldin A / Q000037:antagonists & inhibitors*; D002352:Carrier Proteins / Q000378:metabolism*; D020756:Coatomer Protein / Q000378:metabolism; D003600:Cytosol / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D006056:Golgi Apparatus / Q000187:drug effects* / Q000378:metabolism; D007425:Intracellular Membranes / Q000187:drug effects* / Q000378:metabolism; D009025:Morpholines / Q000494:pharmacology*; D051381:Rats; D014157:Transcription Factors
D002352:Carrier Proteins; D020756:Coatomer Protein; C119945:Ctbp1 protein, rat; D004791:Enzyme Inhibitors; D009025:Morpholines; D014157:Transcription Factors; D020126:Brefeldin A; D000246:Adenosine Diphosphate Ribose; D000244:Adenosine Diphosphate; C033110:RV 538