@article{10902/9452,
year = {2015},
month = {5},
url = {http://hdl.handle.net/10902/9452},
abstract = {Tubulin proteostasis is regulated by a group of molecular chaperones termed tubulin cofactors (TBC). Whereas tubulin heterodimer formation is well-characterized biochemically, its dissociation pathway is not clearly understood. Here, we carried out biochemical assays to dissect the role of the human TBCE and TBCB chaperones in a-tubulin–b-tubulin dissociation. We used electron microscopy and image processing to determine the three-dimensional structure of the human TBCE, TBCB and a-tubulin (aEB) complex, which is formed upon a-tubulin–b-tubulin heterodimer dissociation by the two chaperones. Docking the atomic structures of domains of these proteins, including the TBCE UBL domain, as we determined by X-ray crystallography, allowed description of the molecular architecture of the aEB complex. We found that heterodimer dissociation is an energy-independent process that takes place through a disruption of the a-tubulin–b-tubulin interface that is caused by a steric interaction between b-tubulin and the TBCE cytoskeleton-associated protein glycine-rich (CAP-Gly) and leucine-rich repeat (LRR) domains. The protruding arrangement of chaperone ubiquitin-like (UBL) domains in the aEB complex suggests that there is a direct interaction of this complex with the proteasome, thus mediating a-tubulin degradation.},
publisher = {Company of Biologists},
publisher = {Journal of Cell Science. 2015 May 1;128(9):1824-34},
title = {The structure of the complex between a-tubulin, TBCE and TBCB reveals a tubulin dimer dissociation mechanism},
author = {Marina, Serna and Carranza Ferrer, Gerardo and Janowski, Robert and Canals, Albert and Coll, Miquel and Zabala Otaño, Juan Carlos and Martín Benito, Jaime and Valpuesta Moralejo, Jose María},
}