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dc.contributor.authorMarina, Serna
dc.contributor.authorCarranza Ferrer, Gerardo 
dc.contributor.authorJanowski, Robert
dc.contributor.authorCanals, Albert
dc.contributor.authorColl, Miquel
dc.contributor.authorZabala Otaño, Juan Carlos 
dc.contributor.authorMartín Benito, Jaime
dc.contributor.authorValpuesta Moralejo, Jose María
dc.contributor.otherUniversidad de Cantabriaes_ES
dc.date.accessioned2016-11-03T15:35:54Z
dc.date.available2016-11-03T15:35:54Z
dc.date.issued2015-05-01
dc.identifier.issn0021-9533
dc.identifier.issn1477-9137
dc.identifier.urihttp://hdl.handle.net/10902/9452
dc.description.abstractTubulin 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.es_ES
dc.format.extent17 p.es_ES
dc.language.isoenges_ES
dc.publisherCompany of Biologistses_ES
dc.rightsAtribución 3.0 Españaes_ES
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/es/*
dc.sourceJournal of Cell Science. 2015 May 1;128(9):1824-34es_ES
dc.subject.otherTubulines_ES
dc.subject.otherProtein degradationes_ES
dc.subject.otherChaperonees_ES
dc.subject.otherFolding cofactores_ES
dc.subject.otherMicrotubulees_ES
dc.subject.otherTBCEes_ES
dc.subject.otherTBCBes_ES
dc.titleThe structure of the complex between a-tubulin, TBCE and TBCB reveals a tubulin dimer dissociation mechanismes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.relation.publisherVersionhttp://jcs.biologists.org/content/128/9/1824es_ES
dc.rights.accessRightsopenAccesses_ES
dc.identifier.DOI10.1242/jcs.167387
dc.type.versionpublishedVersiones_ES


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Atribución 3.0 EspañaExcept where otherwise noted, this item's license is described as Atribución 3.0 España