Evidence map›Paper›PMID 32032506›Full record

ArticleCurrent biology : CB2020

Mechanisms of Motor-Independent Membrane Remodeling Driven by Dynamic Microtubules.

Ruddi Rodríguez-García, Vladimir A Volkov, Chiung-Yi Chen, Eugene A Katrukha, Natacha Olieric, Amol Aher, Ilya Grigoriev, Magdalena Preciado López, Michel O Steinmetz, Lukas C Kapitein and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Current biology : CB, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.3field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
  3. Neuronal Calcium Signaling and Cytoskeletal Dynamics in Neurodegeneration.International journal of molecular sciences · 2026
    Review
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  19. A role for endoplasmic reticulum dynamics in the cellular distribution of microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. Cross-linkers at growing microtubule ends generate forces that drive actin transport.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 5 institutions in 2 countries.

Ruddi Rodríguez-GarcíaCell Biology, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, Utrecht 3584, the Netherlands.
Vladimir A VolkovDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, Van der Maasweg 9, Delft 2629, the Netherlands.
Chiung-Yi ChenCell Biology, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, Utrecht 3584, the Netherlands.
Eugene A KatrukhaCell Biology, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, Utrecht 3584, the Netherlands.
Natacha OliericLaboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, Forschungsstrasse 111, Villigen 5232, Switzerland.
Amol AherCell Biology, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, Utrecht 3584, the Netherlands.
Ilya GrigorievCell Biology, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, Utrecht 3584, the Netherlands.
Magdalena Preciado LópezDepartment of Living Matter, AMOLF, Science Park 104, Amsterdam 1098, the Netherlands.
Michel O SteinmetzLaboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, Forschungsstrasse 111, Villigen 5232, Switzerland; University of Basel, Biozentrum, Klingelbergstrasse, Basel 4056, Switzerland.
Lukas C KapiteinCell Biology, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, Utrecht 3584, the Netherlands.
Gijsje KoenderinkDepartment of Living Matter, AMOLF, Science Park 104, Amsterdam 1098, the Netherlands.
Marileen DogteromDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, Van der Maasweg 9, Delft 2629, the Netherlands. Electronic address: m.dogterom@tudelft.nl.
Anna AkhmanovaCell Biology, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, Utrecht 3584, the Netherlands. Electronic address: a.akhmanova@uu.nl.
Utrecht University · NLDelft University of Technology · NLInstitute for Atomic and Molecular Physics · NLPaul Scherrer Institute · CHUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubule-dependent organization of membranous organelles occurs through motor-based pulling and by coupling microtubule dynamics to membrane remodeling. For example, tubules of endoplasmic reticulum (ER) can be extended by kinesin- and dynein-mediated transport and through the association with the tips of dynamic microtubules. The binding between ER and growing microtubule plus ends requires End Binding (EB) proteins and the transmembrane protein STIM1, which form a tip-attachment complex (TAC), but it is unknown whether these proteins are sufficient for membrane remodeling. Furthermore, EBs and their partners undergo rapid turnover at microtubule ends, and it is unclear how highly transient protein-protein interactions can induce load-bearing processive motion. Here, we reconstituted membrane tubulation in a minimal system with giant unilamellar vesicles, dynamic microtubules, an EB protein, and a membrane-bound protein that can interact with EBs and microtubules. We showed that these components are sufficient to drive membrane remodeling by three mechanisms: membrane tubulation induced by growing microtubule ends, motor-independent membrane sliding along microtubule shafts, and membrane pulling by shrinking microtubules. Experiments and modeling demonstrated that the first two mechanisms can be explained by adhesion-driven biased membrane spreading on microtubules. Optical trapping revealed that growing and shrinking microtubule ends can exert forces of ∼0.5 and ∼5 pN, respectively, through attached proteins. Rapidly exchanging molecules that connect membranes to dynamic microtubules can thus bear a sufficient load to induce membrane deformation and motility. Furthermore, combining TAC components and a membrane-attached kinesin in the same in vitro assays demonstrated that they can cooperate in promoting membrane tubule extension.

Indexed as

Endoplasmic ReticulumEscherichia coliEscherichia coli ProteinsKinesinsMembrane ProteinsMicrotubule-Associated ProteinsMicrotubulesEscherichia coli ProteinsKinesinsMembrane ProteinsMicrotubule-Associated ProteinsEB1force generationin vitro reconstitutionkinesinmembranemicrotubuleoptical trapSTIM1+TIPtip-attachement complex

Identifiers

PMID32032506
PMCPMC7090928
OpenAlexW3005339168

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.