Control of microtubule organization and dynamics: Two ends in the limelight
Open accessAbstract
Microtubules have fundamental roles in many essential biological processes, including cell division and intracellular transport. They assemble and disassemble from their two ends, denoted the plus end and the minus end. Significant advances have been made in our understanding of microtubule plus-end-tracking proteins (+TIPs) such as end-binding protein 1 (EB1), XMAP215, selected kinesins and dynein. By contrast, information on microtubule minus-end-targeting proteins (-TIPs), such as the calmodulin-regulated spectrin-associated proteins (CAMSAPs) and Patronin, has only recently started to emerge. Here, we review our current knowledge of factors, including microtubule-targeting agents, that associate with microtubule ends to control the dynamics and function of microtubules during the cell cycle and development.
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EB proteins bind to the tips of polymerizing microtubules and are often used to visualize the subset of dynamic microtubules.
“EB proteins bind to the tips of polymerizing MTs and are often used to visualize the subset of dynamic MTs (Akhmanova and Steinmetz 2015).”
From A live-cell marker to visualize the dynamics of stable microtubules throughout the cell cycle (2023) · cites this paper as Akhmanova and Steinmetz 2015
Mapping revealed that expanded lattice segments were not confined to microtubule ends where GTP-tubulin is typically enriched, but also occurred as discrete patches within the mid-shaft of individual microtubules.
“This mapping revealed that expanded lattice segments were not confined to microtubule ends where GTP-tubulin is typically enriched (Fig. S7, asterisk)49, but also occurred as discrete patches within the mid-shaft of individual microtubules (Fig. 8 and Fig. S7).”
From Ghost Neuron preparation unlocks high-resolution structural mapping of intracellular architecture in axons (2026) · cites this paper as [49]
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Axonal transport: Driving synaptic function
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- Authors
- Akhmanova, A., & Steinmetz, M. O.
- Affiliations
- Utrecht University (NL)
- Paul Scherrer Institute (CH)
- Corresponding author
- Akhmanova, Anna
- Steinmetz, Michel O.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2015-11-12
- Volume
- 16
- Issue
- 12
- Pages
- 711-726
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2237971187
- Cited by
- 895
- References
- 4
- Citations by year
- 2026: 62 · 2025: 59 · 2024: 72 · 2023: 69 · 2022: 92 · 2021: 97 · 2020: 99 · 2019: 105 · 2018: 106 · 2017: 85 · 2016: 47
- FWCI
- 8.00
- Type
- journal article
- Language
- en
- Open access
- green
- dspace.library.uu.nl
- Licence
- other-oa
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- DORA PSI (Paul Scherrer Institute) (submittedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Utrecht University Repository (Utrecht University) (submittedVersion)
- Funders
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- SystemsX.ch
- 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
- microtubule dynamics, microtubule plus ends, microtubule minus ends, plus-end tracking proteins, EB1, XMAP215, kinesin, dynein, Patronin, microtubule inhibitors, cell division, intracellular transport, cell cycle
- MeSH terms
- Animals, Cell Division, Humans, Ligands, Microtubule-Associated Proteins, Microtubules, Protein Binding, Tubulin, Protein Transport, Tubulin Modulators
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