The Library
Spatial positioning of EB family proteins at microtubule tips involves distinct nucleotide-dependent binding properties
Tools
Tools
Tools
Roth, Daniel, Fitton, Benjamin, Chmel, Nikola Paul, Wasiluk, Natalia and Straube, Anne (2018) Spatial positioning of EB family proteins at microtubule tips involves distinct nucleotide-dependent binding properties. Journal of Cell Science, 132 . jcs219550. doi:10.1242/jcs.219550 ISSN 0021-9533.
|
PDF
WRAP-spacial-positioning-family-proteins-microtubule-nucleotide-Roth-2018.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (13Mb) | Preview |
Official URL: https://doi.org/10.1242/jcs.219550
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.
| Item Type: | Journal Article | ||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Subjects: | Q Science > QH Natural history Q Science > QP Physiology |
||||||||||||||||||
| Divisions: | Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences > Cell & Developmental Biology Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School |
||||||||||||||||||
| Library of Congress Subject Headings (LCSH): | Microtubules, Nucleotides, Mutagenesis, Amino acids, Tubulins, Proteins | ||||||||||||||||||
| Journal or Publication Title: | Journal of Cell Science | ||||||||||||||||||
| Publisher: | The Company of Biologists Ltd. | ||||||||||||||||||
| ISSN: | 0021-9533 | ||||||||||||||||||
| Official Date: | 31 October 2018 | ||||||||||||||||||
| Dates: |
|
||||||||||||||||||
| Volume: | 132 | ||||||||||||||||||
| Article Number: | jcs219550 | ||||||||||||||||||
| DOI: | 10.1242/jcs.219550 | ||||||||||||||||||
| Status: | Peer Reviewed | ||||||||||||||||||
| Publication Status: | Published | ||||||||||||||||||
| Access rights to Published version: | Open Access (Creative Commons) | ||||||||||||||||||
| Date of first compliant deposit: | 1 October 2018 | ||||||||||||||||||
| Date of first compliant Open Access: | 2 October 2018 | ||||||||||||||||||
| RIOXX Funder/Project Grant: |
|
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
Downloads
Downloads per month over past year
