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Título

The structure of the TBCE/TBCB chaperones and a-tubulin complex shows a tubulin dimer dissociation mechanism

AutorSerna, Marina; Carranza, Gerardo; Martín-Benito, Jaime; Janowski, Robert ; Canals, Albert ; Coll, Miquel ; Zabala, Juan Carlos; Valpuesta, José María
Palabras claveMicrotubule
Folding cofactor
Chaperone
TBCB
Tubulin
Protein degradation
TBCE
Fecha de publicación14-may-2015
EditorCompany of Biologists
CitaciónJournal of Cell Science 128(9): 1824-1834 (2015)
Resumenubulin 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. © 2015. Published by The Company of Biologists Ltd.
Versión del editorhttp://dx.doi.org/10.1242/jcs.167387
URIhttp://hdl.handle.net/10261/136515
DOI10.1242/jcs.167387
Identificadoresdoi: 10.1242/jcs.167387
issn: 0021-9533
e-issn: 1477-9137
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