scholarly journals Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6

2003 ◽  
Vol 22 (5) ◽  
pp. 1125-1133 ◽  
Author(s):  
Sarah M. Garrard ◽  
Christopher T. Capaldo ◽  
Lin Gao ◽  
Michael K. Rosen ◽  
Ian G. Macara ◽  
...  
Keyword(s):  
Cell Polarity ◽  
Binding Domain ◽  
Gtpase Binding Domain

scholarly journals The exomer cargo adaptor structure reveals a novel GTPase-binding domain

2012 ◽  
Vol 31 (21) ◽  
pp. 4191-4203 ◽  
Author(s):  
Jon E Paczkowski ◽  
Brian C Richardson ◽  
Amanda M Strassner ◽  
J Christopher Fromme
Keyword(s):  
Binding Domain ◽  
Gtpase Binding Domain

Structure of Cdc42 in complex with the GTPase-binding domain of the ‘Wiskott–Aldrich syndrome’ protein

Nature ◽  
10.1038/20726 ◽  
1999 ◽  
Vol 399 (6734) ◽  
pp. 379-383 ◽  
Author(s):  
Norzehan Abdul-Manan ◽  
Behzad Aghazadeh ◽  
Grace A. Liu ◽  
Ananya Majumdar ◽  
Ouathek Ouerfelli ◽  
...  
Keyword(s):  
Binding Domain ◽  
Wiskott Aldrich Syndrome ◽  
Gtpase Binding Domain ◽  
Syndrome Protein

scholarly journals Insights into Oncogenic Mutations of Plexin-B1 Based on the Solution Structure of the Rho GTPase Binding Domain

Structure ◽  
2008 ◽  
Vol 16 (2) ◽  
pp. 246-258 ◽  
Author(s):  
Yufeng Tong ◽  
Prasanta K. Hota ◽  
Mehdi Bagheri Hamaneh ◽  
Matthias Buck
Keyword(s):  
Solution Structure ◽  
Rho Gtpase ◽  
Binding Domain ◽  
Oncogenic Mutations ◽  
Gtpase Binding Domain

scholarly journals EphA4 Signaling Regulates Blastomere Adhesion in the Xenopus Embryo by Recruiting Pak1 to Suppress Cdc42 Function

2007 ◽  
Vol 18 (3) ◽  
pp. 1030-1043 ◽  
Author(s):  
Nicolas Bisson ◽  
Luc Poitras ◽  
Alexander Mikryukov ◽  
Michel Tremblay ◽  
Tom Moss
Keyword(s):  
Catalytic Activity ◽  
Cell Adhesion ◽  
Cell Sorting ◽  
Ectopic Expression ◽  
Binding Domain ◽  
Dominant Negative ◽  
Membrane Targeting ◽  
Dependent Manner ◽  
Eph Receptors ◽  
Gtpase Binding Domain

The control of cell adhesion is an important mechanism by which Eph receptors regulate cell sorting during development. Activation of EphA4 in Xenopus blastulae induces a reversible, cell autonomous loss-of-adhesion and disruption of the blastocoel roof. We show this phenotype is rescued by Nckβ (Grb4) dependent on its interaction with EphA4. Xenopus p21Cdc42/Rac-activated kinase xPAK1 interacts with Nck, is activated in embryo by EphA4 in an Nck-dependent manner, and is required for EphA4-induced loss-of-adhesion. Ectopic expression of xPAK1 phenocopies EphA4 activation. This does not require the catalytic activity of xPAK1, but it does require its GTPase binding domain and is enhanced by membrane targeting. Indeed, membrane targeting of the GTPase binding domain (GBD) of xPAK1 alone is sufficient to phenocopy EphA4 loss-of-adhesion. Both EphA4 and the xPAK1-GBD down-regulate RhoA-GTP levels, and consistent with this, loss-of-adhesion can be rescued by activated Cdc42, Rac, and RhoA and can be epistatically induced by dominant-negative RhoA. Despite this, neither Cdc42 nor Rac activities are down-regulated by EphA4 activation or by the xPAK1-GBD. Together, the data suggest that EphA4 activation sequesters active Cdc42 and in this way down-regulates cell–cell adhesion. This novel signaling pathway suggests a mechanism for EphA4-guided migration.

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

Nature ◽  
10.1038/20732 ◽  
1999 ◽  
Vol 399 (6734) ◽  
pp. 384-388 ◽  
Author(s):  
Helen R. Mott ◽  
Darerca Owen ◽  
Daniel Nietlispach ◽  
Peter N. Lowe ◽  
Edward Manser ◽  
...  
Keyword(s):  
G Protein ◽  
Binding Domain ◽  
Small G Protein ◽  
Gtpase Binding Domain

scholarly journals Structure, Dynamics, Lipid Binding, and Physiological Relevance of the Putative GTPase-binding Domain of Dictyostelium Formin C

2011 ◽  
Vol 286 (42) ◽  
pp. 36907-36920 ◽  
Author(s):  
Sonja A. Dames ◽  
Alexander Junemann ◽  
Hans J. Sass ◽  
André Schönichen ◽  
Barbara E. Stopschinski ◽  
...  
Keyword(s):  
Lipid Binding ◽  
Binding Domain ◽  
Structure Dynamics ◽  
Physiological Relevance ◽  
Gtpase Binding Domain
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