Furthermore, we demonstrated in vitro and in cells that the EB plus-end tracking behavior depends on the calponin homology domain but does not require dimer formation. Protein depletion and rescue experiments showed that EB1 and EB3, but not EB2, promote persistent microtubule growth by suppressing catastrophes. Here we investigated the roles of the three mammalian EBs in controlling microtubule dynamics and analyzed the domains involved. The Journal of Cell Biology Rockefeller University Press Įnd binding proteins (EBs) are highly conserved core components of microtubule plus-end tracking protein networks. Submitted: 30 July 2008 Accepted: 4 February 2009 Footnotes Abbreviations used in this paper: CH, calponin homology DIC, differential interference contrast EB, end binding protein HA, hemagglutinin IP, immunoprecipitation MT, microtubule +TIPs, microtubule plus-end tracking proteins TIRFM, total internal reflection fluorescence microscopy. This probably occurs through their action on microtubule ends, because catastrophe suppression does not require the EB domains needed for binding to known EB partners. When microtubule dynamics is reconstituted with purified tubulin, EBs promote rather than inhibit catastrophes, suggesting that in cells EBs prevent catastrophes by counteracting other microtubule regulators. In contrast, dimerization is necessary for the EB anti-catastrophe activity in cells this explains why the EB1 dimerization domain, which disrupts native EB dimers, exhibits a dominant-negative effect.
Akhmanova, AnnaĮnd binding proteins (EBs) are highly conserved core components of microtubule plus-end tracking protein networks. Grigoriev, Ilya Gouveia, Susana Montenegro Munteanu, E. Mammalian end binding proteins control persistent microtubule growth Mammalian end binding proteins control persistent microtubule growth
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