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Biomol NMR Assign
2016 Oct 01;102:407-11. doi: 10.1007/s12104-016-9677-8.
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(1)H, (13)C and (15)N resonance assignments of the Cdc42-binding domain of TOCA1.
Watson JR
,
Nietlispach D
,
Owen D
,
Mott HR
.
???displayArticle.abstract??? TOCA1 is a downstream effector protein of the small GTPase, Cdc42. It is a multi-domain protein that includes a membrane binding F-BAR domain, a homology region 1 (HR1) domain, which binds selectively to active Cdc42 and an SH3 domain. TOCA1 is involved in the regulation of actin dynamics in processes such as endocytosis, filopodia formation, neurite elongation, cell motility and invasion. Structural insight into the interaction between TOCA1 and Cdc42 will contribute to our understanding of the role of TOCA1 in actin dynamics. The (1)H, (15)N and (13)C NMR backbone and sidechain resonance assignment of the HR1 domain (12 kDa) presented here provides the foundation for structural studies of the domain and its interactions.
Fig. 1. A 15N-HSQC recorded on 13C, 15N-labelled TOCA1 HR1 domain in 20 mM sodium phosphate pH 7.5, 150 mM NaCl, 5 mM DTT, 5 mM MgCl2, recorded at 500 MHz at 25 °C
Fig. 2. Secondary structure summary of the TOCA1 HR1 domain. Black bars indicate NOEs for each of the atoms listed. The height of the bar represents the strength of the NOE. The atoms listed depict the following NOEs: dαN (dαδ) = CαH of residue i and the NH of residue i + 1, or CδH of i + 1 in the case of Prolines; dNN(dNδ,dδN) = NH of residue i and the NH of residue i + 1, or CδH in the case of Prolines; dβN (dβδ) = CβH of residue i and either the NH or CδH (Prolines) of residue i + 1. For the last four rows, dxy (i,i + z) is used, where x and y denote the atoms in residues i and i + z respectively. The Chemical Shift Index value (CSI) is calculated from all of the backbone atom chemical shifts. A value of +1 indicates a β-strand and a value of â1 indicates an α-helix. The secondary structure was predicted from the chemical shifts using TALOS-N (Shen and Bax 2013) and is depicted as a cartoon below the CSI. This figure was generated in CCPN ANALYSIS (Vranken et al. 2005)
Aspenström,
A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton.
1997, Pubmed
Aspenström,
A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton.
1997,
Pubmed
Bai,
A TOCA/CDC-42/PAR/WAVE functional module required for retrograde endocytic recycling.
2015,
Pubmed
Bu,
Cdc42 interaction with N-WASP and Toca-1 regulates membrane tubulation, vesicle formation and vesicle motility: implications for endocytosis.
2010,
Pubmed
Bu,
The Toca-1-N-WASP complex links filopodial formation to endocytosis.
2009,
Pubmed
Chander,
Transducer of Cdc42-dependent actin assembly promotes breast cancer invasion and metastasis.
2013,
Pubmed
Ferentz,
NMR spectroscopy: a multifaceted approach to macromolecular structure.
2000,
Pubmed
Fricke,
Drosophila Cip4/Toca-1 integrates membrane trafficking and actin dynamics through WASP and SCAR/WAVE.
2009,
Pubmed
Gallop,
Phosphoinositides and membrane curvature switch the mode of actin polymerization via selective recruitment of toca-1 and Snx9.
2013,
Pubmed
,
Xenbase
Giuliani,
Requirements for F-BAR proteins TOCA-1 and TOCA-2 in actin dynamics and membrane trafficking during Caenorhabditis elegans oocyte growth and embryonic epidermal morphogenesis.
2009,
Pubmed
Henne,
Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature.
2007,
Pubmed
Ho,
Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex.
2004,
Pubmed
,
Xenbase
Hu,
Transducer of Cdc42-dependent actin assembly promotes epidermal growth factor-induced cell motility and invasiveness.
2011,
Pubmed
Hutchinson,
Differential binding of RhoA, RhoB, and RhoC to protein kinase C-related kinase (PRK) isoforms PRK1, PRK2, and PRK3: PRKs have the highest affinity for RhoB.
2013,
Pubmed
Itoh,
Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins.
2005,
Pubmed
Kakimoto,
Regulation of neuronal morphology by Toca-1, an F-BAR/EFC protein that induces plasma membrane invagination.
2006,
Pubmed
Kobashigawa,
The NMR structure of the TC10- and Cdc42-interacting domain of CIP4.
2009,
Pubmed
Lee,
Self-assembly of filopodia-like structures on supported lipid bilayers.
2010,
Pubmed
,
Xenbase
Maesaki,
The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1.
1999,
Pubmed
Modha,
The Rac1 polybasic region is required for interaction with its effector PRK1.
2008,
Pubmed
Nietlispach,
A novel approach for the sequential backbone assignment of larger proteins: selective intra-HNCA and DQ-HNCA.
2002,
Pubmed
Shen,
Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks.
2013,
Pubmed
Tsujita,
Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis.
2006,
Pubmed
Vranken,
The CCPN data model for NMR spectroscopy: development of a software pipeline.
2005,
Pubmed
Watson,
Erratum to: (1)H, (13)C and (15)N resonance assignments of the Cdc42-binding domain of TOCA1.
2016,
Pubmed
