Tuba
<StructureSection load='4cc2' size='340' side='right' caption='Human Tuba 6th SH3 domain (grey) complex with N-WASP peptide (green), glycerol and Cl- ion (PDB code 4cc2)' scene=>
FunctionFunction
Tuba or dynamin-binding protein is a scaffold protein found in brain synapses which brings together dynamin and actin regulatory proteins. The N-terminal SH3 domains bind dynamin and the C-terminal SH3 domain binds actin regulatory proteins[1]. For more details see Schubert lab: bacterial InIC disrupts human Tuba complexes.
DiseaseDisease
Tuba deficiency causes and abnormal renal ciliary and morphogenetic phenotype. Tuba has a critical role in ciliogenesis and nephrogenesis by regulating Cdc42 activity[2].
Structural highlightsStructural highlights
Tuba contains 6 SH3 domains. The C-terminal 6th SH3 domain binds proline-rich regions of human actin regulating proteins such as N-WASP and Mena. The peptide forms a polyproline type II helix. The interactions of Tuba with the peptide is via SH3-conserved residues[3].
Tuba 3D structuresTuba 3D structures
ReferencesReferences
- ↑ Salazar MA, Kwiatkowski AV, Pellegrini L, Cestra G, Butler MH, Rossman KL, Serna DM, Sondek J, Gertler FB, De Camilli P. Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton. J Biol Chem. 2003 Dec 5;278(49):49031-43. Epub 2003 Sep 22. PMID:14506234 doi:http://dx.doi.org/10.1074/jbc.M308104200
- ↑ Baek JI, Kwon SH, Zuo X, Choi SY, Kim SH, Lipschutz JH. Dynamin Binding Protein (Tuba) Deficiency Inhibits Ciliogenesis and Nephrogenesis in Vitro and in Vivo. J Biol Chem. 2016 Apr 15;291(16):8632-43. doi: 10.1074/jbc.M115.688663. Epub 2016, Feb 19. PMID:26895965 doi:http://dx.doi.org/10.1074/jbc.M115.688663
- ↑ Polle L, Rigano LA, Julian R, Ireton K, Schubert WD. Structural Details of Human Tuba Recruitment by InlC of Listeria monocytogenes Elucidate Bacterial Cell-Cell Spreading. Structure. 2013 Dec 10. pii: S0969-2126(13)00429-2. doi:, 10.1016/j.str.2013.10.017. PMID:24332715 doi:http://dx.doi.org/10.1016/j.str.2013.10.017