The bacterial effector VopL organizes actin into filament-like structures

Jacob A. Zahm; Shae B. Padrick; Zhucheng Chen; Chi W. Pak; Ali A. Yunus; Lisa Henry; Diana R. Tomchick; Zhe Chen; Michael K. Rosen

doi:10.1016/j.cell.2013.09.019

The bacterial effector VopL organizes actin into filament-like structures

Jacob A. Zahm, Shae B. Padrick, Zhucheng Chen, Chi W. Pak, Ali A. Yunus, Lisa Henry, Diana R. Tomchick, Zhe Chen, Michael K. Rosen

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

38 Scopus citations

Abstract

VopL is an effector protein from Vibrio parahaemolyticus that nucleates actin filaments. VopL consists of a VopL C-terminal domain (VCD) and an array of three WASP homology 2 (WH2) motifs. Here, we report the crystal structure of the VCD dimer bound to actin. The VCD organizes three actin monomers in a spatial arrangement close to that found in the canonical actin filament. In this arrangement, WH2 motifs can be modeled into the binding site of each actin without steric clashes. The data suggest a mechanism of nucleation wherein VopL creates filament-like structures, organized by the VCD with monomers delivered by the WH2 array, that can template addition of new subunits. Similarities with Arp2/3 complex and formin proteins suggest that organization of monomers into filament-like structures is a general and central feature of actin nucleation. PaperFlick

Original language	English (US)
Pages (from-to)	423-434
Number of pages	12
Journal	Cell
Volume	155
Issue number	2
DOIs	https://doi.org/10.1016/j.cell.2013.09.019
State	Published - Oct 10 2013

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1016/j.cell.2013.09.019

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title = "The bacterial effector VopL organizes actin into filament-like structures",

abstract = "VopL is an effector protein from Vibrio parahaemolyticus that nucleates actin filaments. VopL consists of a VopL C-terminal domain (VCD) and an array of three WASP homology 2 (WH2) motifs. Here, we report the crystal structure of the VCD dimer bound to actin. The VCD organizes three actin monomers in a spatial arrangement close to that found in the canonical actin filament. In this arrangement, WH2 motifs can be modeled into the binding site of each actin without steric clashes. The data suggest a mechanism of nucleation wherein VopL creates filament-like structures, organized by the VCD with monomers delivered by the WH2 array, that can template addition of new subunits. Similarities with Arp2/3 complex and formin proteins suggest that organization of monomers into filament-like structures is a general and central feature of actin nucleation. PaperFlick",

author = "Zahm, {Jacob A.} and Padrick, {Shae B.} and Zhucheng Chen and Pak, {Chi W.} and Yunus, {Ali A.} and Lisa Henry and Tomchick, {Diana R.} and Zhe Chen and Rosen, {Michael K.}",

note = "Funding Information: We thank Dr. Luke Rice for discussion and assistance with crystallographic model building and refinement, Dr. Dominika Borek for assistance with crystallographic data processing, and Lynda Doolittle for assistance with actin assembly assays. Work was supported by the Howard Hughes Medical Institute and grants from the NIH (R01-GM56322) and Welch Foundation (I-1544). Results shown in this report are derived from work performed at the Argonne National Laboratory, Structural Biology Center at the Advanced Photon Source. Argonne is operated by UChicago Argonne for the U.S. Department of Energy Office of Biological and Environmental Research under contract DE-AC02-06CH11357. ",

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AU - Zahm, Jacob A.

AU - Padrick, Shae B.

AU - Chen, Zhucheng

AU - Pak, Chi W.

AU - Yunus, Ali A.

AU - Henry, Lisa

AU - Tomchick, Diana R.

AU - Chen, Zhe

AU - Rosen, Michael K.

N1 - Funding Information: We thank Dr. Luke Rice for discussion and assistance with crystallographic model building and refinement, Dr. Dominika Borek for assistance with crystallographic data processing, and Lynda Doolittle for assistance with actin assembly assays. Work was supported by the Howard Hughes Medical Institute and grants from the NIH (R01-GM56322) and Welch Foundation (I-1544). Results shown in this report are derived from work performed at the Argonne National Laboratory, Structural Biology Center at the Advanced Photon Source. Argonne is operated by UChicago Argonne for the U.S. Department of Energy Office of Biological and Environmental Research under contract DE-AC02-06CH11357.

PY - 2013/10/10

Y1 - 2013/10/10

N2 - VopL is an effector protein from Vibrio parahaemolyticus that nucleates actin filaments. VopL consists of a VopL C-terminal domain (VCD) and an array of three WASP homology 2 (WH2) motifs. Here, we report the crystal structure of the VCD dimer bound to actin. The VCD organizes three actin monomers in a spatial arrangement close to that found in the canonical actin filament. In this arrangement, WH2 motifs can be modeled into the binding site of each actin without steric clashes. The data suggest a mechanism of nucleation wherein VopL creates filament-like structures, organized by the VCD with monomers delivered by the WH2 array, that can template addition of new subunits. Similarities with Arp2/3 complex and formin proteins suggest that organization of monomers into filament-like structures is a general and central feature of actin nucleation. PaperFlick

AB - VopL is an effector protein from Vibrio parahaemolyticus that nucleates actin filaments. VopL consists of a VopL C-terminal domain (VCD) and an array of three WASP homology 2 (WH2) motifs. Here, we report the crystal structure of the VCD dimer bound to actin. The VCD organizes three actin monomers in a spatial arrangement close to that found in the canonical actin filament. In this arrangement, WH2 motifs can be modeled into the binding site of each actin without steric clashes. The data suggest a mechanism of nucleation wherein VopL creates filament-like structures, organized by the VCD with monomers delivered by the WH2 array, that can template addition of new subunits. Similarities with Arp2/3 complex and formin proteins suggest that organization of monomers into filament-like structures is a general and central feature of actin nucleation. PaperFlick

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The bacterial effector VopL organizes actin into filament-like structures

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