2l3l

Publication Abstract from PubMed

Human Tubulin Binding Cofactor C (TBCC) is a post-chaperonin involved in the folding and assembly of alpha- and beta-tubulin monomers leading to the release of productive tubulin heterodimers ready to polymerize into microtubules. In this process it collaborates with other cofactors (TBC's A, B, D, and E) and forms a supercomplex with TBCD, beta-tubulin, TBCE and alpha-tubulin. Here, we demonstrate that TBCC depletion results in multipolar spindles and mitotic failure. Accordingly, TBCC is found at the centrosome and is implicated in bipolar spindle formation. We also determine by NMR the structure of the N-terminal domain of TBCC. The TBCC N-terminal domain adopts a spectrin-like fold topology composed of a left-handed 3-stranded alpha-helix bundle. Remarkably, the 30-residue N-terminal segment of the TBCC N-terminal domain is flexible and disordered in solution. This unstructured region is involved in the interaction with tubulin. Our data lead us to propose a testable model for TBCC N-terminal domain/tubulin recognition in which the highly charged N-terminus as well as residues from the three helices and the loops interact with the acidic hypervariable regions of tubulin monomers.

The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.,Garcia-Mayoral MF, Castano R, Fanarraga ML, Zabala JC, Rico M, Bruix M PLoS One. 2011;6(10):e25912. doi: 10.1371/journal.pone.0025912. Epub 2011 Oct 18. PMID:22028797^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.