Stimulation of endogenous ADP-ribosylation by brefeldin A

Maria Antonietta De Matteis, Maria Di Girolamo, Antonino Colanzi, Merce Pallas, Giuseppe Di Tullio, Lee J. Mcdonald, Joel Moss, Giovanna Santini, Sergei Bannykh, Daniela Corda, Alberto Luini

Research output: Contribution to journalArticlepeer-review


Brefeldin A (BFA) is a fungal metabolite that exerts profound and generally inhibitory actions on membrane transport. At least some of the BFA effects are due to inhibition of the GDP-GTP exchange on the ADP-ribosylation factor (ARF) catalyzed by membrane protein(s). ARF activation is likely to be a key event in the association of non-clathrin coat components, including ARF itself, onto transport organelles. ARF, in addition to participating in membrane transport, is known to function as a cofactor in the enzymatic activity of cholera toxin, a bacterial ADP-ribosyltransferase. In this study we have examined whether BFA, in addition to inhibiting membrane transport, might affect endogenous ADP-ribosylation in eukaryotic cells. Two cytosolic proteins of 38 and 50 kDa were enzymatically ADP-ribosylated in the presence of BFA in cellular extracts. The 38-kDa substrate was tentatively identified as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase. The BFA- binding components mediating inhibition of membrane traffic and stimulation of ADP-ribosylation appear to have the same ligand specificity. These data demonstrate the existence of a BFA-sensitive mono(ADP-ribosyl)transferase that may play a role in membrane movements.

Original languageEnglish
Pages (from-to)1114-1118
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number3
Publication statusPublished - Feb 1 1994

ASJC Scopus subject areas

  • Genetics
  • General


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