Publication Type Journal Article
Title Autoinhibition of TBCB regulates EB1-mediated microtubule dynamics
Authors Gerardo Carranza Raquel Castano Monica L. Fanarraga Juan Carlos Villegas Joao Goncalves M. H. A. Soares Jesus Avila Marco Marenchino Ramon Campos-Olivas Guillermo Montoya Juan Carlos Zabala
Groups
Journal CELLULAR AND MOLECULAR LIFE SCIENCES
Year 2013
Month January
Volume 70
Number 2
Pages 357-371
Abstract Tubulin cofactors (TBCs) participate in the folding, dimerization, and dissociation pathways of the tubulin dimer. Among them, TBCB and TBCE are two CAP-Gly domain-containing proteins that together efficiently interact with and dissociate the tubulin dimer. In the study reported here we showed that TBCB localizes at spindle and midzone microtubules during mitosis. Furthermore, the motif DEI/M-COO- present in TBCB, which is similar to the EEY/F-COO- element characteristic of EB proteins, CLIP-170, and alpha-tubulin, is required for TBCE-TBCB heterodimer formation and thus for tubulin dimer dissociation. This motif is responsible for TBCB autoinhibition, and our analysis suggests that TBCB is a monomer in solution. Mutants of TBCB lacking this motif are derepressed and induce microtubule depolymerization through an interaction with EB1 associated with microtubule tips. TBCB is also able to bind to the chaperonin complex CCT containing alpha-tubulin, suggesting that it could escort tubulin to facilitate its folding and dimerization, recycling or degradation.
DOI http://dx.doi.org/10.1007/s00018-012-1114-2
ISBN
Publisher
Book Title
ISSN 1420-682X
EISSN
Conference Name
Bibtex ID ISI:000313018100010
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