Evidence map›Paper›PMID 34031406›Full record

ArticleNature communications2021

Cryo-EM structure of cortical microtubules from human parasite Toxoplasma gondii identifies their microtubule inner proteins.

Xiangli Wang, Yong Fu, Wandy L Beatty, Meisheng Ma, Alan Brown, L David Sibley, Rui Zhang

Erratum issuedAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
–field-weighted citation impact
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

47 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Microtubule inner proteins in apicomplexan parasites.Biochemical Society transactions · 2026
    Review
  10. The essential function of the apical polar ring during the blood stage ofbioRxiv : the preprint server for biology · 2026
    Article
  11. Article
  12. Atomic models of the Toxoplasma cell invasion machinery.Nature structural & molecular biology · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. Microtubule inner proteins ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Luminal acetylation of microtubules is not essential forMicrobial cell (Graz, Austria) · 2025
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Xiangli Wang *Department of Biochemistry and Molecular Biophysics, Washington University in St. Louis, School of Medicine, St. Louis, MO, USA.
Yong Fu *Department of Molecular Microbiology, Washington University in St. Louis, School of Medicine, St. Louis, MO, USA.
Wandy L BeattyDepartment of Molecular Microbiology, Washington University in St. Louis, School of Medicine, St. Louis, MO, USA.
Meisheng MaDepartment of Biochemistry and Molecular Biophysics, Washington University in St. Louis, School of Medicine, St. Louis, MO, USA.
Alan BrownDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0002-0021-0476
L David SibleyDepartment of Molecular Microbiology, Washington University in St. Louis, School of Medicine, St. Louis, MO, USA. sibley@wustl.edu.
Rui ZhangDepartment of Biochemistry and Molecular Biophysics, Washington University in St. Louis, School of Medicine, St. Louis, MO, USA. zhangrui@wustl.edu.ORCID http://orcid.org/0000-0003-3159-9565

Funding

PROTEIN SECRETION &INTRACELLULAR SURVIVAL BY TOXOPLASMAR01AI034036 · NIAID · WASHINGTON UNIVERSITY · PI SIBLEY, L. DAVID · 1993 to 2019
$7.9M
Regulation of host cell egress by Toxoplasma gondiiR01AI162749 · NIAID · WASHINGTON UNIVERSITY · PI SIBLEY, L. DAVID · 2022 to 2025
$3.1M
Mechanoregulation of Ciliary MotilityR01GM141109 · NIGMS · HARVARD MEDICAL SCHOOL · PI BROWN, ALAN · 2021 to 2025
$2.1M
NIAID NIH HHS R01 AI034036NIAID NIH HHS R01 AI162749NIGMS NIH HHS R01 GM141109
6 · The paper itself

Abstract

In living cells, microtubules (MTs) play pleiotropic roles, which require very different mechanical properties. Unlike the dynamic MTs found in the cytoplasm of metazoan cells, the specialized cortical MTs from Toxoplasma gondii, a prevalent human pathogen, are extraordinarily stable and resistant to detergent and cold treatments. Using single-particle cryo-EM, we determine their ex vivo structure and identify three proteins (TrxL1, TrxL2 and SPM1) as bona fide microtubule inner proteins (MIPs). These three MIPs form a mesh on the luminal surface and simultaneously stabilize the tubulin lattice in both longitudinal and lateral directions. Consistent with previous observations, deletion of the identified MIPs compromises MT stability and integrity under challenges by chemical treatments. We also visualize a small molecule like density at the Taxol-binding site of β-tubulin. Our results provide the structural basis to understand the stability of cortical MTs and suggest an evolutionarily conserved mechanism of MT stabilization from the inside.

Indexed as

Cryoelectron MicroscopyBinding SitesCRISPR-Cas SystemsHost-Parasite InteractionsHumansMicrotubule-Associated ProteinsMicrotubule ProteinsMicrotubulesPaclitaxelToxoplasmaTubulinMicrotubule-Associated ProteinsMicrotubule ProteinsPaclitaxelTubulin

Identifiers

PMID34031406
PMCPMC8144581

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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.