Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

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.

[img]
Preview
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

Request Changes to record.

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:
DateEvent
31 October 2018Published
27 September 2018Available
20 September 2018Accepted
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:
Project/Grant IDRIOXX Funder NameFunder ID
UNSPECIFIED[EPSRC] Engineering and Physical Sciences Research Councilhttp://dx.doi.org/10.13039/501100000266
UNSPECIFIEDMarie Curie Cancer Carehttp://dx.doi.org/10.13039/501100000654
UNSPECIFIEDLister Institute of Preventive Medicinehttp://dx.doi.org/10.13039/501100001255
RPG-2016-260Leverhulme Trusthttp://dx.doi.org/10.13039/501100000275
200870/Z/16/ZWellcome Trusthttp://dx.doi.org/10.13039/100010269

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item

Downloads

Downloads per month over past year

View more statistics

twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us