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          Institute: MPI für molekulare Zellbiologie und Genetik     Collection: Publikationen MPI-CBG 2009 arch     Display Documents



ID: 463263.0, MPI für molekulare Zellbiologie und Genetik / Publikationen MPI-CBG 2009 arch
EB1 recognizes the nucleotide state of tubulin in the microtubule lattice
Authors:Zanic, Marija; Stear, Jeffrey H; Hyman, Anthony A; Howard, Jonathon
Date of Publication (YYYY-MM-DD):2009
Title of Journal:PLoS ONE
Volume:4
Issue / Number:10
Start Page:e7585-1
End Page:e7585-5
Copyright:not available
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:Plus-end-tracking proteins (+TIPs) are localized at the fast-growing, or plus end, of microtubules, and link microtubule ends to cellular structures. One of the best studied +TIPs is EB1, which forms comet-like structures at the tips of growing microtubules. The molecular mechanisms by which EB1 recognizes and tracks growing microtubule ends are largely unknown. However, one clue is that EB1 can bind directly to a microtubule end in the absence of other proteins. Here we use an in vitro assay for dynamic microtubule growth with two-color total-internal-reflection-fluorescence imaging to investigate binding of mammalian EB1 to both stabilized and dynamic microtubules. We find that under conditions of microtubule growth, EB1 not only tip tracks, as previously shown, but also preferentially recognizes the GMPCPP microtubule lattice as opposed to the GDP lattice. The interaction of EB1 with the GMPCPP microtubule lattice depends on the E-hook of tubulin, as well as the amount of salt in solution. The ability to distinguish different nucleotide states of tubulin in microtubule lattice may contribute to the end-tracking mechanism of EB1.
External Publication Status:published
Document Type:Article
Communicated by:n.n.
Affiliations:MPI für molekulare Zellbiologie und Genetik
Identifiers:LOCALID:1363
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