Structural mechanism of WASP activation by the enterohaemorrhagic E. coli effector EspFU (Q27651305)

identical protein binding

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

Hui-Chun Cheng

1

0 references

Brian M Skehan

2

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Kenneth G Campellone

3

0 references

John M Leong

4

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Michael K Rosen

Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome

5

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language of work or name

English

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publication date

21 August 2008

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published in

Nature

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volume

454

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issue

7207

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page(s)

1009-13

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cites work

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Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization

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Characterization of TccP-mediated N-WASP activation during enterohaemorrhagic Escherichia coli infection

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Actin binding to the central domain of WASP/Scar proteins plays a critical role in the activation of the Arp2/3 complex

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The nucleotide switch in Cdc42 modulates coupling between the GTPase-binding and allosteric equilibria of Wiskott-Aldrich syndrome protein

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TccP is an enterohaemorrhagic Escherichia coli O157:H7 type III effector protein that couples Tir to the actin-cytoskeleton

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Contingent phosphorylation/dephosphorylation provides a mechanism of molecular memory in WASP.

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Enterohemorrhagic Escherichia coli O157:H7 produces Tir, which is translocated to the host cell membrane but is not tyrosine phosphorylated.

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Enterohaemorrhagic Escherichia coli Tir requires a C-terminal 12-residue peptide to initiate EspF-mediated actin assembly and harbours N-terminal sequences that influence pedestal length.

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EspFU is a translocated EHEC effector that interacts with Tir and N-WASP and promotes Nck-independent actin assembly

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A two-state allosteric model for autoinhibition rationalizes WASP signal integration and targeting

27 November 2018

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A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex

27 November 2018

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A tyrosine-phosphorylated 12-amino-acid sequence of enteropathogenic Escherichia coli Tir binds the host adaptor protein Nck and is required for Nck localization to actin pedestals

27 November 2018

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Global disruption of the WASP autoinhibited structure on Cdc42 binding. Ligand displacement as a novel method for monitoring amide hydrogen exchange.

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Methods to measure actin polymerization

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12 December 2020

Host-pathogen interactions: a diversity of themes, a variety of molecular machines

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12 December 2020

A robust and cost-effective method for the production of Val, Leu, Ile (delta 1) methyl-protonated 15N-, 13C-, 2H-labeled proteins

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12 December 2020

Four-dimensional carbon-13/carbon-13-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: application to interleukin 1.beta

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12 December 2020

Structure of the N-WASP EVH1 Domain-WIP Complex

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Crossref

https://api.crossref.org/works/10.1038%2FNATURE07160

7 January 2021

inferred from DOI database lookup

Production and Incorporation of15N,13C,2H (1H-δ1 Methyl) Isoleucine into Proteins for Multidimensional NMR Studies

1 reference

Crossref

https://api.crossref.org/works/10.1038%2FNATURE07160

7 January 2021