(Q47244406)

12 January 2018

title

Chemical inhibition of N-WASP by stabilization of a native autoinhibited conformation (English)

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12 January 2018

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5

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author name string

Jeffrey R Peterson

1

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Lincoln C Bickford

2

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David Morgan

3

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Annette S Kim

4

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Marc W Kirschner

6

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Michael K Rosen

7

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publication date

4 July 2004

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12 January 2018

Nature Structural & Molecular Biology

published in

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12 January 2018

volume

11

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issue

8

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page(s)

747-755

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12 January 2018

https://scigraph.springernature.com/pub.10.1038/nsmb796

exact match

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cites work

Allosteric drugs: thinking outside the active-site box.

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Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex

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The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42

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Corequirement of specific phosphoinositides and small GTP-binding protein Cdc42 in inducing actin assembly in Xenopus egg extracts

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A chemical inhibitor of N-WASP reveals a new mechanism for targeting protein interactions

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The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly

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

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Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate

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Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein

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Actin assembly mediated by Arp2/3 complex and WASP family proteins.

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

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Regulation of Wiskott-Aldrich syndrome protein and related molecules

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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.

31 March 2020

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

31 March 2020

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Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex

31 March 2020

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Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway

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A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42

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GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex

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Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP

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Sustained activation of N-WASP through phosphorylation is essential for neurite extension

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How signaling proteins integrate multiple inputs: a comparison of N-WASP and Cdk2.

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Signal transduction. Autoinhibition control

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Autoinhibitory domains: modular effectors of cellular regulation

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Autoinhibited proteins as promising drug targets

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AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR

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31 March 2020

Identifiers

DOI

10.1038/NSMB796

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12 January 2018

Dimensions Publication ID

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12 January 2018