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

Article Abstract:

GTPases Cdc42, Rac and Rho operate as molecular switches in signalling pathways regulating cytoskeletal architecture, progression of cell cycle and gene expression. The Wiskott-Aldrich syndrome protein (WASP) is thought to link activation of Cdc42 to the rearrangement of actin. Human mutations in WASP lead to severe haematopoletic cell function defects. A minimal GTPase-binding domain (GBD) from WASP is reported, and it is suggested that GBD-sequence divergence outside of the CRIB motif could reflect further regulatory interactions.

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C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases

Article Abstract:

Research shows that Rho GDP-dissocation inhibitors (GDIs) have inhibitory and binding functions that are attributable to two areas of the protein which are structurally different. Nucleotide dissociation from the Rho-family member Cdc42 is inhibited by RhoGDI's unstructured amino-terminal region. The rate at which nucleotides dissociate from the GTPase is not greatly affected by the carboxy-terminal folded domain which binds to Cdc42.

G proteins, Letter to the Editor, Dissociation, Dissociation reactions

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Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein

Article Abstract:

The Rho-family GTPase, Cdc42 can control the actin cytoskeleton via activation of Wiskott-Aldrich syndrome protein (WASP) family members. The autoinhibited structure of the GTPase-binding domain of WASP can be induced by the C-terminal region. Binding of Cdc42 to the GTPase-binding domain leads to dramatic conformational changes, leading to disruption of the hydrophobic core.

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