ArticleNature chemical biology2021
A molecular trap inside microtubules probes luminal access by soluble proteins.
Article in Nature chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Microtubule posttranslational modifications provide unique recognition patterns for associated proteins.The EMBO journal · 2026Article
- A genetically encoded microtubule bundler for causal dissection of microtubule bundling in cells.bioRxiv : the preprint server for biology · 2026Article
- Systematic identification of microtubule lumen proteins reveals a taxane-sensitive luminal resident JPT2 regulating MEC17 accessibility.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Development and Recent Advances in SLIPT-PM: A Chemogenetic Platform for Manipulating Signaling at the Plasma Membrane.Chembiochem : a European journal of chemical biology · 2025Review
- Maspin/SerpinB5 is a cytoskeleton-binding protein that regulates epithelial cell shape.Communications biology · 2025Article
- Multi-Target Biological Activities of Podophyllotoxin-Derived Natural Products.Oncology research · 2025Review
- Lumenal components of cytoplasmic microtubules.Biochemical Society transactions · 2022Review
- Posttranslational modifications of the cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2021Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The uniquely hollow structure of microtubules (MTs) confers characteristic mechanical and biological properties. Although most regulatory processes take place at the outer surface, molecular events inside MTs, such as α-tubulin acetylation, also play a critical role. However, how regulatory proteins reach the site of action remains obscure. To assess luminal accessibility, we first identified luminally positioned residues of β-tubulin that can be fused to a protein of interest. We then developed a chemically inducible technique with which cytosolic proteins can be rapidly trapped at the lumen of intact MTs in cells. A luminal trapping assay revealed that soluble proteins of moderate size can enter the lumen via diffusion through openings at the MT ends and sides. Additionally, proteins forming a complex with tubulins can be incorporated to the lumen through the plus ends. Our approach may not only illuminate this understudied territory, but may also help understand its roles in MT-mediated functions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.