Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem-W domain nucleation

Pathogen proteins targeting the actin cytoskeleton often serve as model systems to understand their more complex eukaryotic analogs. We show that the strong actin filament nucleation activity of Vibrio VopL depends on its three W domains and dimerization through a unique VopL C-terminal domain (VCD)...

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Main Authors:	Namgoong, Suk, Boczkowska, Malgorzata, Glista, Michael J., Winkelman, Jonathan D., Rebowski, Grzegorz, Kovar, David R., Dominguez, Roberto
Format:	Online
Language:	English
Published:	2011
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3173040/

id	pubmed-3173040
recordtype	oai_dc
spelling	pubmed-31730402012-03-01 Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem-W domain nucleation Namgoong, Suk Boczkowska, Malgorzata Glista, Michael J. Winkelman, Jonathan D. Rebowski, Grzegorz Kovar, David R. Dominguez, Roberto Article Pathogen proteins targeting the actin cytoskeleton often serve as model systems to understand their more complex eukaryotic analogs. We show that the strong actin filament nucleation activity of Vibrio VopL depends on its three W domains and dimerization through a unique VopL C-terminal domain (VCD). The VCD displays a novel all-helical fold and interacts with the pointed end of the actin nucleus, contributing to the nucleation activity directly and through duplication of the W domain repeat. VopL promotes rapid cycles of filament nucleation and detachment, but generally has no effect on elongation. Profilin inhibits VopL-induced nucleation by competing for actin binding to the W domains. Combined, the results suggest that VopL stabilizes a hexameric double-stranded pointed end nucleus. Analysis of hybrid constructs of VopL and the eukaryotic nucleator Spire suggest that Spire may also function as a dimer in cells. 2011-08-28 /pmc/articles/PMC3173040/ /pubmed/21873985 http://dx.doi.org/10.1038/nsmb.2109 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Namgoong, Suk Boczkowska, Malgorzata Glista, Michael J. Winkelman, Jonathan D. Rebowski, Grzegorz Kovar, David R. Dominguez, Roberto
spellingShingle	Namgoong, Suk Boczkowska, Malgorzata Glista, Michael J. Winkelman, Jonathan D. Rebowski, Grzegorz Kovar, David R. Dominguez, Roberto Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem-W domain nucleation
author_facet	Namgoong, Suk Boczkowska, Malgorzata Glista, Michael J. Winkelman, Jonathan D. Rebowski, Grzegorz Kovar, David R. Dominguez, Roberto
author_sort	Namgoong, Suk
title	Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem-W domain nucleation
title_short	Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem-W domain nucleation
title_full	Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem-W domain nucleation
title_fullStr	Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem-W domain nucleation
title_full_unstemmed	Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem-W domain nucleation
title_sort	mechanism of actin filament nucleation by vibrio vopl and implications for tandem-w domain nucleation
description	Pathogen proteins targeting the actin cytoskeleton often serve as model systems to understand their more complex eukaryotic analogs. We show that the strong actin filament nucleation activity of Vibrio VopL depends on its three W domains and dimerization through a unique VopL C-terminal domain (VCD). The VCD displays a novel all-helical fold and interacts with the pointed end of the actin nucleus, contributing to the nucleation activity directly and through duplication of the W domain repeat. VopL promotes rapid cycles of filament nucleation and detachment, but generally has no effect on elongation. Profilin inhibits VopL-induced nucleation by competing for actin binding to the W domains. Combined, the results suggest that VopL stabilizes a hexameric double-stranded pointed end nucleus. Analysis of hybrid constructs of VopL and the eukaryotic nucleator Spire suggest that Spire may also function as a dimer in cells.
publishDate	2011
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3173040/
_version_	1611475616303939584

Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem-W domain nucleation

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