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

doi:10.1016/S0014-5793(99)01269-7

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

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Abstract

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 language	English
Pages (from-to)	310-312
Number of pages	3
Journal	FEBS Letters
Volume	459
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(99)01269-7
Publication status	Published - Oct 15 1999

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Keywords

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

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abstract = "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.",

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AU - De Matteis, Maria Antonieta

AU - Luna, Ana

AU - Di Tullio, Giuseppe

AU - Corda, Daniela

AU - Kok, Jan Willem

AU - Luini, Alberto

AU - Egea, Gustavo

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N2 - 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.

AB - 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.

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KW - Membrane transport

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10.1016/S0014-5793(99)01269-7