TBCD

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.

TBCD has been shown to interact with ARL2.{{cite journal | vauthors = Shern JF, Sharer JD, Pallas DC, Bartolini F, Cowan NJ, Reed MS, Pohl J, Kahn RA | title = Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A | journal = J. Biol. Chem. | volume = 278 | issue = 42 | pages = 40829–36 | date = October 2003 | pmid = 12912990 | doi = 10.1074/jbc.M308678200 | doi-access = free }}{{cite journal | vauthors = Bhamidipati A, Lewis SA, Cowan NJ | title = ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin | journal = J. Cell Biol. | volume = 149 | issue = 5 | pages = 1087–96 | date = May 2000 | pmid = 10831612 | pmc = 2174823 | doi = 10.1083/jcb.149.5.1087 }}

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