Tubulin-specific chaperone D is a protein that in humans is encoded by the TBCD gene. 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. [provided by RefSeq]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications.
Tubulin-folding protein; involved in the first step of the tubulin folding pathway. Modulates microtubule dynamics by capturing GTP-bound beta-tubulin (TUBB). Acts as a GTPase-activating protein (GAP) for ARL2. Its ability to interact with beta tubulin is regulated via its interaction with ARL2. Induces microtubule disruption in absence of ARL2. Increases degradation of beta tubulin, when overexpressed in polarized cells. Promotes epithelial cell detachment, a process antagonized by ARL2. Induces tight adherens and tight junctions disassembly at the lateral cell membrane.