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The structure of the complex between α-tubulin, TBCE and TBCB reveals a tubulin dimer dissociation mechanism

AuthorsSerna, Marina; Carranza, Gerardo; Martín-Benito, Jaime; Janowski, Robert ; Canals, Albert ; Coll, Miquel ; Zabala, Juan Carlos; Valpuesta, José María
Folding cofactor
Protein degradation
Issue Date2015
PublisherCompany of Biologists
CitationJournal of Cell Science 128(9): 1824-1834 (2015)
Abstract© 2015. Published by The Company of Biologists Ltd. 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 α-tubulin-β-tubulin dissociation. We used electron microscopy and image processing to determine the three-dimensional structure of the human TBCE, TBCB and α-tubulin (αEB) complex, which is formed upon α-tubulin-β-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 α-tubulin-β-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 α-tubulin degradation.
Publisher version (URL)http://dx.doi.org/10.1242/jcs.167387
Identifiersdoi: 10.1242/jcs.167387
issn: 1477-9137
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