PDMP blocks the BFA-induced ADP-ribosylation of BARS-50 in isolated Golgi membranes

Maria Antonieta De Matteis, Ana Luna, Giuseppe Di Tullio, Daniela Corda, Jan Willem Kok, Alberto Luini, Gustavo Egea

Research output: Contribution to journalArticle


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 β-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. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)310-312
Number of pages3
JournalFEBS Letters
Issue number3
Publication statusPublished - Oct 15 1999



  • ADP-ribosylation
  • Brefeldin A
  • D,L-Threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol
  • Golgi complex
  • Membrane transport

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

De Matteis, M. A., Luna, A., Di Tullio, G., Corda, D., Kok, J. W., Luini, A., & Egea, G. (1999). PDMP blocks the BFA-induced ADP-ribosylation of BARS-50 in isolated Golgi membranes. FEBS Letters, 459(3), 310-312. https://doi.org/10.1016/S0014-5793(99)01269-7