Spatial positioning of EB family proteins at microtubule tips involves distinct nucleotide-dependent binding properties

• DOI: 10.1242/jcs.219550
• Publication Date: 2018-09-27T10:15:20Z
• Authors: Daniel Roth; Benjamin P. Fitton; Nikola P. Chmel; Natalia Wasiluk; Anne Straube
• Keywords: 0301 basic medicine; Binding Sites; Nucleotides; QH; QP; Microtubules; 03 medical and health sciences; Protein Domains; Tubulin; Humans; Microtubule-Associated Proteins; Research Article; Protein Binding; Signal Transduction

EB proteins track the ends of growing microtubules and regulate microtubule dynamics both directly by acting as hub tip-tracking network. Mammalian cells express cell type-specific combinations three with different cellular roles. Here, we reconstitute EB1, EB2 EB3 tip tracking in vitro We find that all EBs show rapid exchange at their signal correlates to assembly rate. However, signals differ maxima position from tip. Using built nucleotide analogues site-directed mutagenesis, prefers binding lattices containing a 1:1 mixture nucleotides its distinct specificity is conferred amino acid substitutions right-hand-side interface microtubule-binding domain tubulin. Our data are consistent model paralogues sense state β-tubulins flanking site. Their profile preferred sites contributes occupying spatially domains temporally evolving structure.