A viral protein that blocks Arf1-mediated COP-I assembly by inhibiting the guanine nucleotide exchange factor GBF1

Els Wessels; Daniël Duijsings; Ting-Kuang Niu; Steffi Neumann; Viola M Oorschot; Frank de Lange; Kjerstin H W Lanke; Judith Klumperman; Andreas Henke; Catherine L Jackson; Willem J G Melchers; Frank J M van Kuppeveld

doi:10.1016/j.devcel.2006.06.005

A viral protein that blocks Arf1-mediated COP-I assembly by inhibiting the guanine nucleotide exchange factor GBF1

Els Wessels, Daniël Duijsings, Ting-Kuang Niu, Steffi Neumann, Viola M Oorschot, Frank de Lange, Kjerstin H W Lanke, Judith Klumperman, Andreas Henke, Catherine L Jackson, Willem J G Melchers, Frank J M van Kuppeveld

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

Many viruses modify cellular processes for their own benefit. The enterovirus 3A protein inhibits endoplasmic reticulum (ER)-to-Golgi transport, a function previously suggested to be important for viral suppression of immune responses. Here, we show that a virus carrying a 3A protein defective in inhibiting ER-to-Golgi transport is indeed less virulent in mice, and we unravel the mechanism by which 3A inhibits this trafficking step. Evidence is provided that 3A inhibits the activation of the GTPase ADP-ribosylation factor 1 (Arf1), which regulates the recruitment of the COP-I coat complex to membranes. 3A specifically inhibits the function of GBF1, a guanine nucleotide exchange factor for Arf1, by interacting with its N terminus. By specifically interfering with GBF1-mediated Arf1 activation, 3A may prove a valuable tool in dissecting the early steps of the secretory pathway.

Original language	English
Pages (from-to)	191-201
Number of pages	11
Journal	Developmental Cell
Volume	11
Issue number	2
DOIs	https://doi.org/10.1016/j.devcel.2006.06.005
Publication status	Published - Aug 2006

Keywords

ADP-Ribosylation Factor 1
Animals
Cell Line
Cell Membrane
Cercopithecus aethiops
Coat Protein Complex I
Endoplasmic Reticulum
Golgi Apparatus
Guanine Nucleotide Exchange Factors
Mice
Models, Animal
Protein Transport
Viral Proteins

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10.1016/j.devcel.2006.06.005

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Wessels, E., Duijsings, D., Niu, T.-K., Neumann, S., Oorschot, V. M., de Lange, F., Lanke, K. H. W., Klumperman, J., Henke, A., Jackson, C. L., Melchers, W. J. G., & van Kuppeveld, F. J. M. (2006). A viral protein that blocks Arf1-mediated COP-I assembly by inhibiting the guanine nucleotide exchange factor GBF1. Developmental Cell, 11(2), 191-201. https://doi.org/10.1016/j.devcel.2006.06.005

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title = "A viral protein that blocks Arf1-mediated COP-I assembly by inhibiting the guanine nucleotide exchange factor GBF1",

abstract = "Many viruses modify cellular processes for their own benefit. The enterovirus 3A protein inhibits endoplasmic reticulum (ER)-to-Golgi transport, a function previously suggested to be important for viral suppression of immune responses. Here, we show that a virus carrying a 3A protein defective in inhibiting ER-to-Golgi transport is indeed less virulent in mice, and we unravel the mechanism by which 3A inhibits this trafficking step. Evidence is provided that 3A inhibits the activation of the GTPase ADP-ribosylation factor 1 (Arf1), which regulates the recruitment of the COP-I coat complex to membranes. 3A specifically inhibits the function of GBF1, a guanine nucleotide exchange factor for Arf1, by interacting with its N terminus. By specifically interfering with GBF1-mediated Arf1 activation, 3A may prove a valuable tool in dissecting the early steps of the secretory pathway.",

keywords = "ADP-Ribosylation Factor 1, Animals, Cell Line, Cell Membrane, Cercopithecus aethiops, Coat Protein Complex I, Endoplasmic Reticulum, Golgi Apparatus, Guanine Nucleotide Exchange Factors, Mice, Models, Animal, Protein Transport, Viral Proteins",

author = "Els Wessels and Dani{\"e}l Duijsings and Ting-Kuang Niu and Steffi Neumann and Oorschot, {Viola M} and {de Lange}, Frank and Lanke, {Kjerstin H W} and Judith Klumperman and Andreas Henke and Jackson, {Catherine L} and Melchers, {Willem J G} and {van Kuppeveld}, {Frank J M}",

year = "2006",

month = aug,

doi = "10.1016/j.devcel.2006.06.005",

language = "English",

volume = "11",

pages = "191--201",

journal = "Developmental Cell",

issn = "1534-5807",

publisher = "Cell Press",

number = "2",

}

Wessels, E, Duijsings, D, Niu, T-K, Neumann, S, Oorschot, VM, de Lange, F, Lanke, KHW, Klumperman, J, Henke, A, Jackson, CL, Melchers, WJG & van Kuppeveld, FJM 2006, 'A viral protein that blocks Arf1-mediated COP-I assembly by inhibiting the guanine nucleotide exchange factor GBF1', Developmental Cell, vol. 11, no. 2, pp. 191-201. https://doi.org/10.1016/j.devcel.2006.06.005

TY - JOUR

T1 - A viral protein that blocks Arf1-mediated COP-I assembly by inhibiting the guanine nucleotide exchange factor GBF1

AU - Wessels, Els

AU - Duijsings, Daniël

AU - Niu, Ting-Kuang

AU - Neumann, Steffi

AU - Oorschot, Viola M

AU - de Lange, Frank

AU - Lanke, Kjerstin H W

AU - Klumperman, Judith

AU - Henke, Andreas

AU - Jackson, Catherine L

AU - Melchers, Willem J G

AU - van Kuppeveld, Frank J M

PY - 2006/8

Y1 - 2006/8

N2 - Many viruses modify cellular processes for their own benefit. The enterovirus 3A protein inhibits endoplasmic reticulum (ER)-to-Golgi transport, a function previously suggested to be important for viral suppression of immune responses. Here, we show that a virus carrying a 3A protein defective in inhibiting ER-to-Golgi transport is indeed less virulent in mice, and we unravel the mechanism by which 3A inhibits this trafficking step. Evidence is provided that 3A inhibits the activation of the GTPase ADP-ribosylation factor 1 (Arf1), which regulates the recruitment of the COP-I coat complex to membranes. 3A specifically inhibits the function of GBF1, a guanine nucleotide exchange factor for Arf1, by interacting with its N terminus. By specifically interfering with GBF1-mediated Arf1 activation, 3A may prove a valuable tool in dissecting the early steps of the secretory pathway.

AB - Many viruses modify cellular processes for their own benefit. The enterovirus 3A protein inhibits endoplasmic reticulum (ER)-to-Golgi transport, a function previously suggested to be important for viral suppression of immune responses. Here, we show that a virus carrying a 3A protein defective in inhibiting ER-to-Golgi transport is indeed less virulent in mice, and we unravel the mechanism by which 3A inhibits this trafficking step. Evidence is provided that 3A inhibits the activation of the GTPase ADP-ribosylation factor 1 (Arf1), which regulates the recruitment of the COP-I coat complex to membranes. 3A specifically inhibits the function of GBF1, a guanine nucleotide exchange factor for Arf1, by interacting with its N terminus. By specifically interfering with GBF1-mediated Arf1 activation, 3A may prove a valuable tool in dissecting the early steps of the secretory pathway.

KW - ADP-Ribosylation Factor 1

KW - Animals

KW - Cell Line

KW - Cell Membrane

KW - Cercopithecus aethiops

KW - Coat Protein Complex I

KW - Endoplasmic Reticulum

KW - Golgi Apparatus

KW - Guanine Nucleotide Exchange Factors

KW - Mice

KW - Models, Animal

KW - Protein Transport

KW - Viral Proteins

U2 - 10.1016/j.devcel.2006.06.005

DO - 10.1016/j.devcel.2006.06.005

M3 - Article

C2 - 16890159

SN - 1534-5807

VL - 11

SP - 191

EP - 201

JO - Developmental Cell

JF - Developmental Cell

IS - 2

ER -

A viral protein that blocks Arf1-mediated COP-I assembly by inhibiting the guanine nucleotide exchange factor GBF1

Abstract

Keywords

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