Dynamic behavior of GFP-CLIP-170 reveals fast protein turnover on microtubule plus ends
Open accessAbstract
Microtubule (MT) plus end-tracking proteins (+TIPs) specifically recognize the ends of growing MTs. +TIPs are involved in diverse cellular processes such as cell division, cell migration, and cell polarity. Although +TIP tracking is important for these processes, the mechanisms underlying plus end specificity of mammalian +TIPs are not completely understood. Cytoplasmic linker protein 170 (CLIP-170), the prototype +TIP, was proposed to bind to MT ends with high affinity, possibly by copolymerization with tubulin, and to dissociate seconds later. However, using fluorescence-based approaches, we show that two +TIPs, CLIP-170 and end-binding protein 3 (EB3), turn over rapidly on MT ends. Diffusion of CLIP-170 and EB3 appears to be rate limiting for their binding to MT plus ends. We also report that the ends of growing MTs contain a surplus of sites to which CLIP-170 binds with relatively low affinity. We propose that the observed loss of fluorescent +TIPs at plus ends does not reflect the behavior of single molecules but is a result of overall structural changes of the MT end.
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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 [17]
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Mammalian end binding proteins control persistent microtubule growth
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- Authors
- Dragestein, K. A., van Cappellen, W. A., van Haren, J., Tsibidis, G. D., Akhmanova, A., Knoch, T. A., Grosveld, F., & Galjart, N.
- Affiliations
- 1Department of Cell Biology and Genetics
- 2Department of Reproduction and Development, Erasmus Medical Center, 3000 DR Rotterdam, Netherlands
- Foundation for Research and Technology Hellas (GR)
- Corresponding author
- Galjart, Niels
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2008-02-18
- Volume
- 180
- Issue
- 4
- Pages
- 729-737
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2265578
- OpenAlex
- W2129158700
- Cited by
- 116
- References
- 30
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 4 · 2022: 3 · 2021: 3 · 2020: 2 · 2019: 6 · 2018: 4 · 2017: 5 · 2016: 5 · 2015: 5 · 2014: 14 · 2013: 7 · 2012: 7
- FWCI
- 6.85
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- EUR Research Repository (Erasmus University Rotterdam) (publishedVersion)
- EUR Research Repository (Erasmus University Rotterdam) (submittedVersion)
- RePub (Erasmus University Rotterdam) (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- CLIP-170, EB3, microtubule plus ends, plus-end tracking proteins, protein turnover, diffusion-limited binding, GFP fusion protein, cell polarity
- MeSH terms
- Animals, Binding Sites, Chlorocebus aethiops, HeLa Cells, Humans, Mice, Transgenic, Microtubule-Associated Proteins, Microtubules, Neoplasm Proteins, Protein Binding, Recombinant Fusion Proteins, Time Factors, COS Cells, Amino Acid Motifs, Protein Transport, Green Fluorescent Proteins, Mice, Rats
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