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Cited by 475Microtubule and mitosis dynamicsCellular Mechanics and InteractionsCancer Treatment and Pharmacology

Reconstitution of a microtubule plus-end tracking system in vitro

Bieling, Peter, Laan, Liedewij, Schek, Henry, Munteanu, E. Laura, Sandblad, Linda, Dogterom, Marileen, Brunner, Damian, Surrey, Thomas·2007·Nature
DOI 10.1038/nature06386
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Abstract

The microtubule cytoskeleton is essential to cell morphogenesis. Growing microtubule plus ends have emerged as dynamic regulatory sites in which specialized proteins, called plus-end-binding proteins (+TIPs), bind and regulate the proper functioning of microtubules. However, the molecular mechanism of plus-end association by +TIPs and their ability to track the growing end are not well understood. Here we report the in vitro reconstitution of a minimal plus-end tracking system consisting of the three fission yeast proteins Mal3, Tip1 and the kinesin Tea2. Using time-lapse total internal reflection fluorescence microscopy, we show that the EB1 homologue Mal3 has an enhanced affinity for growing microtubule end structures as opposed to the microtubule lattice. This allows it to track growing microtubule ends autonomously by an end recognition mechanism. In addition, Mal3 acts as a factor that mediates loading of the processive motor Tea2 and its cargo, the Clip170 homologue Tip1, onto the microtubule lattice. The interaction of all three proteins is required for the selective tracking of growing microtubule plus ends by both Tea2 and Tip1. Our results dissect the collective interactions of the constituents of this plus-end tracking system and show how these interactions lead to the emergence of its dynamic behaviour. We expect that such in vitro reconstitutions will also be essential for the mechanistic dissection of other plus-end tracking systems.

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Crossref · 10.1038/nature06386

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  • EBs and their partners, including MCAK, exchange rapidly on binding sites at microtubule tips, whereas the sites themselves turn over relatively slowly.

    “This finding supports the view that the EBs and their partners, including MCAK, exchange rapidly on the binding sites at MT tips (dwell times of 1 s or less), whereas the sites themselves turn over relatively slowly (on the order of several seconds) [12, 17].”

    From In vitro reconstitution of the functional interplay between MCAK and EB3 at microtubule plus ends (2010) · cites this paper as [12]

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Authors
Bieling, P., Laan, L., Schek, H., Munteanu, E. L., Sandblad, L., Dogterom, M., Brunner, D., & Surrey, T.
Affiliations
  • European Molecular Biology Laboratory (DE)
  • Institute for Atomic and Molecular Physics (NL)
Corresponding author
  • Dogterom, Marileen
  • Brunner, Damian
  • Surrey, Thomas
ORCID
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2007-12
Volume
450
Issue
7172
Pages
1100-1105
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
DOI
10.1038/nature06386
OpenAlex
W2027382153
Cited by
475
References
30
Citations by year
2026: 12 · 2025: 8 · 2024: 13 · 2023: 19 · 2022: 23 · 2021: 26 · 2020: 21 · 2019: 35 · 2018: 29 · 2017: 29 · 2016: 27 · 2015: 29 · 2014: 34 · 2013: 26 · 2012: 26
FWCI
11.17
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)
Locations
  • Nature (publishedVersion)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
  • MPG.PuRe (Max Planck Society) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
  • Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
Keywords
microtubule plus-end tracking, TIP1, microtubule dynamics, Schizosaccharomyces pombe, in vitro reconstitution, microtubule lattice
MeSH terms
Cell-Free System, Heat-Shock Proteins, Intermediate Filament Proteins, Microscopy, Fluorescence, Microtubule-Associated Proteins, Microtubules, Schizosaccharomyces, Schizosaccharomyces pombe Proteins

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