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Search results 101 to 123 out of 123 for Tbca

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0.018s
Type Details Score
Protein Domain
Type: Homologous_superfamily
Description: The tubulin heterodimer consists of one alpha- and one beta-tubulin polypeptide. In humans, five tubulin-specific chaperones termed TBCA/B/C/D/E are essential for bring the alpha- and beta-tubulin subunits together into a tightly associated heterodimer. Following the generation of quasi-native beta- and alpha-tubulin polypeptides (via multiple rounds of ATP-dependent interaction with the cytosolic chaperonin), TBCA and TBCB bind to and stabilise newly synthesised beta- and alpha-tubulin, respectively. The exchange of beta-tubulin between TBCA and TBCD, and of alpha-tubulin between TBCB and TBCE, resulting in the formation of TBCD/beta and TBCE/alpha. These two complexes then interact with each other and form a supercomplex (TBCE/alpha/TBCD/beta). Interaction of the supercomplex with TBCC causes the disassembly of the supercomplex and the release of E-site GDP-bound alpha/beta tubulin heterodimer, which becomes polymerization competent following spontaneous exchange with GTP [].This entry represents tubulin binding cofactor A (TBCA) from animal, plants and fungi. Human TBCA functions as a molecular chaperone for beta-tubulin []. Budding yeast TBCA, also known as Rbl2, may bind transiently to free beta-tubulin, which then passes into an aggregated form that is not toxic []. The sequence identity of Rbl2 and human TBCA is only 32%, they appear to be structurally distinct and may interact with beta-tubulin by different mechanisms []. The structure of TBCA has three helices forming a bundle closed fold with left-handed twist topology going up-and-down.
Publication
First Author: Yu H
Year: 2022
Journal: Commun Biol
Title: Maternal diabetes-mediated RORA suppression in mice contributes to autism-like offspring through inhibition of aromatase.
Volume: 5
Issue: 1
Pages: 51
Genotype
Symbol: Gt(ROSA)26Sor/Gt(ROSA)26Sor<+> Tg(Otp-cre)1Hzo/?
Background: involves: 129S4/SvJae * C57BL/6 * FVB/N
Zygosity: cn
Has Mutant Allele: true
Genotype
Symbol: Cic/Cic Tg(Otp-cre)1Hzo/?
Background: involves: C57BL/6 * C57BL/6N * FVB/N
Zygosity: cn
Has Mutant Allele: true
Protein
Organism: Mus musculus/domesticus
Length: 84  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 72  
Fragment?: true
Publication
First Author: Kirik V
Year: 2002
Journal: Curr Biol
Title: Functional analysis of the tubulin-folding cofactor C in Arabidopsis thaliana.
Volume: 12
Issue: 17
Pages: 1519-23
Publication
First Author: Bartolini F
Year: 2002
Journal: J Biol Chem
Title: Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C.
Volume: 277
Issue: 17
Pages: 14629-34
Publication
First Author: Steinborn K
Year: 2002
Journal: Genes Dev
Title: The Arabidopsis PILZ group genes encode tubulin-folding cofactor orthologs required for cell division but not cell growth.
Volume: 16
Issue: 8
Pages: 959-71
Publication
First Author: Mayer U
Year: 1999
Journal: Eur J Cell Biol
Title: Mutations in the pilz group genes disrupt the microtubule cytoskeleton and uncouple cell cycle progression from cell division in Arabidopsis embryo and endosperm.
Volume: 78
Issue: 2
Pages: 100-8
Publication    
First Author: Nithianantham S
Year: 2015
Journal: Elife
Title: Tubulin cofactors and Arl2 are cage-like chaperones that regulate the soluble αβ-tubulin pool for microtubule dynamics.
Volume: 4
Protein Domain
Type: Family
Description: The tubulin heterodimer consists of one alpha- and one beta-tubulin polypeptide. In humans, five tubulin-specific chaperones termed TBCA/B/C/D/E are essential for bring the alpha- and beta-tubulin subunits together into a tightly associated heterodimer. Following the generation of quasi-native beta- and alpha-tubulin polypeptides (via multiple rounds of ATP-dependent interaction with the cytosolic chaperonin), TBCA and TBCB bind to and stabilise newly synthesised beta- and alpha-tubulin, respectively. The exchange of beta-tubulin between TBCA and TBCD, and of alpha-tubulin between TBCB and TBCE, resulting in the formation of TBCD/beta and TBCE/alpha. These two complexes then interact with each other and form a supercomplex (TBCE/alpha/TBCD/beta). Interaction of the supercomplex with TBCC causes the disassembly of the supercomplex and the release of E-site GDP-bound alpha/beta tubulin heterodimer, which becomes polymerization competent following spontaneous exchange with GTP [].This entry represents tubulin-specific chaperone C (TBCC, also known as tubulin-folding cofactor C), which is involved in the final step of the tubulin folding pathway [, ]. In Arabidopsis thaliana, it is required for continuous microtubule cytoskeleton organisation, mitotic division, cytokinesis, and to couple cell cycle progression to cell division in embryos and endosperms [, ].
Protein Domain
Type: Family
Description: The tubulin heterodimer consists of one alpha- and one beta-tubulin polypeptide. In humans, five tubulin-specific chaperones termed TBCA/B/C/D/E are essential for bring the alpha- and beta-tubulin subunits together into a tightly associated heterodimer. Following the generation of quasi-native beta- and alpha-tubulin polypeptides (via multiple rounds of ATP-dependent interaction with the cytosolic chaperonin), TBCA and TBCB bind to and stabilise newly synthesised beta- and alpha-tubulin, respectively. The exchange of beta-tubulin between TBCA and TBCD, and of alpha-tubulin between TBCB and TBCE, resulting in the formation of TBCD/beta and TBCE/alpha. These two complexes then interact with each other and form a supercomplex (TBCE/alpha/TBCD/beta). Interaction of the supercomplex with TBCC causes the disassembly of the supercomplex and the release of E-site GDP-bound alpha/beta tubulin heterodimer, which becomes polymerization competent following spontaneous exchange with GTP [].This entry represents tubulin-folding cofactor D (TBCD) and its homologues. Its ability to interact with beta tubulin is regulated via its interaction with ARL2 (ADP ribosylation factor-like protein 2), a small monomeric G protein. ARL2 inhibits the beta-tubulin GTPase activating protein (GAP) activity of TBCD, and its interaction with native tubulin dimers [, ].
Publication  
First Author: Song W
Year: 2013
Journal: Neuroscience
Title: Globular adiponectin elicits neuroprotection by inhibiting NADPH oxidase-mediated oxidative damage in ischemic stroke.
Volume: 248
Pages: 136-44
Genotype
Symbol: Cic/Cic Gt(ROSA)26Sor/Gt(ROSA)26Sor<+> Tg(Otp-cre)1Hzo/?
Background: involves: 129S4/SvJae * C57BL/6N * FVB/N
Zygosity: cn
Has Mutant Allele: true
Publication  
First Author: Iniaghe LO
Year: 2015
Journal: Neurobiol Dis
Title: Dimethyl fumarate confers neuroprotection by casein kinase 2 phosphorylation of Nrf2 in murine intracerebral hemorrhage.
Volume: 82
Pages: 349-358
Protein
Organism: Mus musculus/domesticus
Length: 352  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: true
Publication
First Author: Bhamidipati A
Year: 2000
Journal: J Cell Biol
Title: ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin.
Volume: 149
Issue: 5
Pages: 1087-96
Protein
Organism: Mus musculus/domesticus
Length: 1196  
Fragment?: false
Publication
First Author: Lu HC
Year: 2017
Journal: Nat Genet
Title: Disruption of the ATXN1-CIC complex causes a spectrum of neurobehavioral phenotypes in mice and humans.
Volume: 49
Issue: 4
Pages: 527-536
Protein
Organism: Mus musculus/domesticus
Length: 341  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 341  
Fragment?: false