2017
DOI: 10.1083/jcb.201612195
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Structural differences between yeast and mammalian microtubules revealed by cryo-EM

Abstract: Yeast MTs do not appear to undergo the lattice compaction seen in mammalian MTs upon GTP hydrolysis. Binding of the +TIP Bim1, both between and within αβ-tubulin dimers, causes compaction of yeast MTs and their rapid disassembly.

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Cited by 77 publications
(87 citation statements)
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References 59 publications
(99 reference statements)
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“…Interestingly, binding of Bim1 to yeast MTs was also distinct from the binding of EB3 to mammalian MTs. While the latter binds MTs with a tubulin dimer repeat, as most MAPs do, Bim1 binds yeast MTs with a tubulin monomer repeat, that is, double the stoichiometry [28]. A similar difference in binding pattern has also been previously observed for the Ndc80 kinetochore complex, which binds with the classical tubulin dimer repeat in C elegans, but with a tubulin monomer repeat in humans [7,20,21,29].…”
Section: Structure Of Mts From Alternative Sourcesmentioning
confidence: 59%
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“…Interestingly, binding of Bim1 to yeast MTs was also distinct from the binding of EB3 to mammalian MTs. While the latter binds MTs with a tubulin dimer repeat, as most MAPs do, Bim1 binds yeast MTs with a tubulin monomer repeat, that is, double the stoichiometry [28]. A similar difference in binding pattern has also been previously observed for the Ndc80 kinetochore complex, which binds with the classical tubulin dimer repeat in C elegans, but with a tubulin monomer repeat in humans [7,20,21,29].…”
Section: Structure Of Mts From Alternative Sourcesmentioning
confidence: 59%
“…With the development of new purification strategies [24] and expression systems [25,26], it has recently become possible to study more pure tubulin samples from alternative sources. A number of recent structural studies have now used recombinant human tubulin [25,27] and purified yeast tubulin [28] (which is significantly simpler in terms of tubulin isoforms). The latter opens the possibility to carry out parallel in vitro and in vivo studies in the characterization of tubulin mutants, as well as to explore, given the evolutionary distance between yeast and mammalian tubulin, the conservation (or not) of different structural properties between these two MT systems.…”
Section: Structure Of Mts From Alternative Sourcesmentioning
confidence: 99%
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“…Our previous purification of TBCD•ARL2 as a dimer that cannot bind GTP [33] is consistent with the binding of β-tubulin acting to change the nucleotide binding properties of the ARL2, specifically promoting GTP binding, which we hypothesize then allosterically alters β-tubulin structure into one that promotes binding to α-tubulin. Finally, there is steadily increasing evidence this work, our previous study [11], and a recent publication [87], that reveal important species differences in tubulins and microtubules that need to be considered when testing hypotheses regarding the complex folding or polymerization pathways.…”
Section: Discussionmentioning
confidence: 91%