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Data show that bovine and human TBCD have functionally identical roles in tubulin (show TUBB ELISA Kits) heterodimer assembly, and that the inability of human TBCD to disrupt microtubule integrity can be overcome by siRNA-mediated suppression of expression of Arl2 (show ARL2 ELISA Kits).
provides first evidence that beta-tubulin cofactor D plays a role in cells independent of its presumed role in folding tubulin (show TUBB ELISA Kits) heterodimers
Cofactor D functions as a centrosomal protein and is required for the recruitment of the gamma-tubulin (show TUBG1 ELISA Kits) 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