Flipping the switch: the structural basis for signaling through the CRIB motif (Q34019126)

30 July 2017

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title

Flipping the switch: the structural basis for signaling through the CRIB motif (English)

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30 July 2017

Hoffman GR

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30 July 2017

Cerione RA

series ordinal

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30 July 2017

language of work or name

English

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publication date

1 August 2000

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30 July 2017

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30 July 2017

volume

102

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30 July 2017

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30 July 2017

page(s)

403-406

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Structure of Cdc42 in complex with the GTPase-binding domain of the 'Wiskott-Aldrich syndrome' protein

30 July 2017

cites work

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Actin polymerization: Where the WASP stings

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A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases

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Actions of Rho family small G proteins and p21-activated protein kinases on mitogen-activated protein kinase family members

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7 January 2021

Structure of the complex of Cdc42Hs with a peptide derived from P-21 activated kinase

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Active and inactive protein kinases: structural basis for regulation

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Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein

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Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch

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A non-receptor tyrosine kinase that inhibits the GTPase activity of p21cdc42

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A brain serine/threonine protein kinase activated by Cdc42 and Rac1

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Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP

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Structure of Cdc42 bound to the GTPase binding domain of PAK

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Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK

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Residues in Cdc42 that specify binding to individual CRIB effector proteins

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The Cdc42/Rac interactive binding region motif of the Wiskott Aldrich syndrome protein (WASP) is necessary but not sufficient for tight binding to Cdc42 and structure formation

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Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization

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Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm

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Cloning and Characterization of a Novel Cdc42-associated Tyrosine Kinase, ACK-2, from Bovine Brain

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Identifiers

DOI

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30 July 2017

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