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Dimeric WH2 domains in Vibrio VopF promote actin filament barbed-end uncapping and assisted elongation
by
Carlier, Marie-France
, Orban, Jozsef
, Avvaru, Balendu Sankara
, Romet-Lemonne, Guillaume
, Jégou, Antoine
, Guichard, Bérengère
, Pernier, Julien
in
631/45/612/1228
/ 631/80/128/1276
/ Actin
/ Actin Capping Proteins - chemistry
/ Actin Capping Proteins - metabolism
/ Actins - chemistry
/ Actins - metabolism
/ Animals
/ Bacterial proteins
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Binding sites
/ Biochemistry
/ Biological Microscopy
/ Crystal structure
/ Life Sciences
/ Membrane Biology
/ Models, Molecular
/ Molecular biology
/ Nucleation
/ Pathogens
/ Peptides
/ Physiological aspects
/ Protein Conformation
/ Protein Interaction Domains and Motifs
/ Protein Multimerization
/ Protein Structure
/ Protein Structure, Quaternary
/ Rabbits
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Structure
/ Vibrio cholerae
/ Vibrio cholerae - genetics
/ Vibrio cholerae - metabolism
/ Vibrio parahaemolyticus
/ Wiskott-Aldrich Syndrome Protein Family - chemistry
/ Wiskott-Aldrich Syndrome Protein Family - genetics
/ Wiskott-Aldrich Syndrome Protein Family - metabolism
2013
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Dimeric WH2 domains in Vibrio VopF promote actin filament barbed-end uncapping and assisted elongation
by
Carlier, Marie-France
, Orban, Jozsef
, Avvaru, Balendu Sankara
, Romet-Lemonne, Guillaume
, Jégou, Antoine
, Guichard, Bérengère
, Pernier, Julien
in
631/45/612/1228
/ 631/80/128/1276
/ Actin
/ Actin Capping Proteins - chemistry
/ Actin Capping Proteins - metabolism
/ Actins - chemistry
/ Actins - metabolism
/ Animals
/ Bacterial proteins
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Binding sites
/ Biochemistry
/ Biological Microscopy
/ Crystal structure
/ Life Sciences
/ Membrane Biology
/ Models, Molecular
/ Molecular biology
/ Nucleation
/ Pathogens
/ Peptides
/ Physiological aspects
/ Protein Conformation
/ Protein Interaction Domains and Motifs
/ Protein Multimerization
/ Protein Structure
/ Protein Structure, Quaternary
/ Rabbits
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Structure
/ Vibrio cholerae
/ Vibrio cholerae - genetics
/ Vibrio cholerae - metabolism
/ Vibrio parahaemolyticus
/ Wiskott-Aldrich Syndrome Protein Family - chemistry
/ Wiskott-Aldrich Syndrome Protein Family - genetics
/ Wiskott-Aldrich Syndrome Protein Family - metabolism
2013
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Dimeric WH2 domains in Vibrio VopF promote actin filament barbed-end uncapping and assisted elongation
by
Carlier, Marie-France
, Orban, Jozsef
, Avvaru, Balendu Sankara
, Romet-Lemonne, Guillaume
, Jégou, Antoine
, Guichard, Bérengère
, Pernier, Julien
in
631/45/612/1228
/ 631/80/128/1276
/ Actin
/ Actin Capping Proteins - chemistry
/ Actin Capping Proteins - metabolism
/ Actins - chemistry
/ Actins - metabolism
/ Animals
/ Bacterial proteins
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Binding sites
/ Biochemistry
/ Biological Microscopy
/ Crystal structure
/ Life Sciences
/ Membrane Biology
/ Models, Molecular
/ Molecular biology
/ Nucleation
/ Pathogens
/ Peptides
/ Physiological aspects
/ Protein Conformation
/ Protein Interaction Domains and Motifs
/ Protein Multimerization
/ Protein Structure
/ Protein Structure, Quaternary
/ Rabbits
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Structure
/ Vibrio cholerae
/ Vibrio cholerae - genetics
/ Vibrio cholerae - metabolism
/ Vibrio parahaemolyticus
/ Wiskott-Aldrich Syndrome Protein Family - chemistry
/ Wiskott-Aldrich Syndrome Protein Family - genetics
/ Wiskott-Aldrich Syndrome Protein Family - metabolism
2013
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Dimeric WH2 domains in Vibrio VopF promote actin filament barbed-end uncapping and assisted elongation
Journal Article
Dimeric WH2 domains in Vibrio VopF promote actin filament barbed-end uncapping and assisted elongation
2013
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Overview
Proteins containing repeats of the WASP homology 2 (WH2) actin-binding module are multifunctional regulators of actin nucleation and assembly. Now biochemical analyses of VopF from
Vibrio cholerae
reveal a new regulatory mechanism of actin-filament barbed-end dynamics including enhanced nucleation, uncapping and assisted elongation.
Proteins containing repeats of the WASP homology 2 (WH2) actin-binding module are multifunctional regulators of actin nucleation and assembly. The bacterial effector VopF in
Vibrio cholerae
, like VopL in
Vibrio parahaemolyticus
, is a unique homodimer of three WH2 motifs linked by a C-terminal dimerization domain. We show that only the first and third WH2 domains of VopF bind G-actin in a non-nucleating, sequestered conformation. Moreover, dimeric WH2 domains in VopF give rise to unprecedented regulation of actin assembly. Specifically, two WH2 domains on opposite protomers of VopF direct filament assembly from actin or profilin–actin by binding terminal subunits and uncapping capping protein from barbed ends by a new mechanism. Thus, VopF does not nucleate filaments by capping a pointed-end F-actin hexamer. These properties may contribute to VopF pathogenicity, and they show how dimeric WH2 peptides may mediate processive filament growth.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Actin
/ Actin Capping Proteins - chemistry
/ Actin Capping Proteins - metabolism
/ Animals
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Peptides
/ Protein Interaction Domains and Motifs
/ Protein Structure, Quaternary
/ Rabbits
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Vibrio cholerae - metabolism
/ Wiskott-Aldrich Syndrome Protein Family - chemistry
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