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TBCD protein was localized in the middle region and in the tail of the sperm while in the oocyte the localization was cytosolic.
Authors conclude that TBCD is a novel functional contributor to the mammalian cerebral cortex development, and that the pathological mechanism resulting from the mutations we describe is likely to involve compromised interactions with one or more TBCD-interacting effectors that influence the dynamics and behaviour of the neuronal cytoskeleton.
conclude that the TBCD*ARL2*beta-tubulin complex represents a functional intermediate in the beta-tubulin folding pathway whose activity is regulated by the cycling of nucleotides on ARL2
Results identified ARL2 and TBCD, as important in tubulin folding and microtubule dynamics. Both ARL2 and TBCD also localize to centrosomes. [review]
variants. We identified two candidate homozygous missense variants, R942Q in the tubulin-folding cofactor D (TBCD) gene and H250Q in the bromo-adjacent homology domain and coiled-coil containing 1 (BAHCC1) gene, located on chromosome 17q25.3 with an interval of 1.4 Mbp.
Intractable epilepsy, intellectual disability and acquired microcephaly, and cortical atrophy and thinned corpus callosum as major MRI features, caused by biallelic variants in TBCD.
findings establish that defective TBCD function underlies a recognizable encephalopathy and drives accelerated microtubule polymerization and enhanced microtubule stability, underscoring an additional cause of altered microtubule dynamics with impact on neuronal function and survival in the developing brain
Defects of microtubule formation caused by TBCD mutations may underlie the pathomechanism of a neurodegenerative encephalopathy.
genetic polymorphism is associated with bone mineral accretion in children with asthma receiving intermittent oral corticosteroids
Data show that bovine and human TBCD have functionally identical roles in tubulin heterodimer assembly, and that the inability of human TBCD to disrupt microtubule integrity can be overcome by siRNA-mediated suppression of expression of Arl2.
provides first evidence that beta-tubulin cofactor D plays a role in cells independent of its presumed role in folding tubulin heterodimers
Cofactor D functions as a centrosomal protein and is required for the recruitment of the gamma-tubulin ring complex at centrosomes and organization of the mitotic spindle
Cofactor D is one of four proteins (cofactors A, D, E, and C) involved in the pathway leading to correctly folded beta-tubulin from folding intermediates. Cofactors A and D are believed to play a role in capturing and stabilizing beta-tubulin intermediates in a quasi-native confirmation. Cofactor E binds to the cofactor D/beta-tubulin complex\; interaction with cofactor C then causes the release of beta-tubulin polypeptides that are committed to the native state.
beta-tubulin cofactor D
, tubulin-folding cofactor D
, tubulin-specific chaperone D