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- W2893327070 abstract "EB proteins track the ends of growing microtubules and regulate microtubule dynamics both directly and by acting as the hub of the tip-tracking network. Mammalian cells express cell type-specific combinations of three EB proteins with different cellular roles. Here we reconstitute EB1, EB2 and EB3 tip tracking in vitro. We find that all three EBs show rapid exchange at the microtubule tip and that their signal correlates to the microtubule assembly rate. However, the three signals differ in their maxima and the position from the microtubule tip. Using microtubules built with nucleotide analogues and site-directed mutagenesis, we show that EB2 prefers binding to microtubule lattices containing a 1:1 mixture of different nucleotides and its distinct binding specificity is conferred by amino acid substitutions at the right-hand side interface of the EB microtubule-binding domain with tubulin. Our data are consistent with the model that all three EB paralogs sense the nucleotide state of both β-tubulins flanking their binding site. Their different profile of preferred binding sites contributes to occupying spatially distinct domains at the temporally evolving microtubule tip structure." @default.
- W2893327070 created "2018-10-05" @default.
- W2893327070 creator A5012957755 @default.
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- W2893327070 date "2018-01-01" @default.
- W2893327070 modified "2023-10-02" @default.
- W2893327070 title "Spatial positioning of EB family proteins at microtubule tips involves distinct nucleotide-dependent binding properties" @default.
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- W2893327070 doi "https://doi.org/10.1242/jcs.219550" @default.
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