Evidence map›Paper›PMID 32773040›Full record

ArticleeLife2020

Cryo-EM structure of VASH1-SVBP bound to microtubules.

Faxiang Li, Yang Li, Xuecheng Ye, Haishan Gao, Zhubing Shi, Xuelian Luo, Luke M Rice, Hongtao Yu

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.4field-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

27 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Mechanisms of microtubule dynamics from single-molecule measurements.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Review
  9. Tubulin detyrosination shapesProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Faxiang Li *Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States.ORCID 0000-0002-6442-9063
Yang Li *Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, United States.
Xuecheng YeDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, United States.
Haishan GaoDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States.ORCID 0000-0002-4954-8793
Zhubing ShiDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States.ORCID 0000-0002-9624-4960
Xuelian LuoDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States.ORCID 0000-0002-5058-4695
Luke M RiceDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, United States.ORCID 0000-0001-6551-3307
Hongtao YuDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States.ORCID 0000-0002-8861-049X
The University of Texas Southwestern Medical Center · USWestlake University · CN

Funding

CONFORMATION & RECOGNITION IN MICROTUBLE DYNAMICSR01GM098543 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI RICE, LUKE W · 2011 to 2023
$4.2M
Keratins as novel determinants of tumor biologyR01CA160255 · NCI · JOHNS HOPKINS UNIVERSITY · PI COULOMBE, PIERRE · 2011 to 2017
$1.9M
Activation mechanism of the tumor-suppressing MST-LATS kinase cascadeR01GM107415 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI LUO, XUELIAN · 2013 to 2016
$1.2M
Cancer Prevention and Research Institute of Texas RP160255Cancer Prevention and Research Institute of Texas RP160667-P2NIGMS NIH HHS R01 GM098543NIGMS NIH HHS R01 GM107415NIH HHS GM098543NIH HHS GM107415Welch Foundation I-1441Welch Foundation I-1908Welch Foundation I-1932
6 · The paper itself

Abstract

The dynamic tyrosination-detyrosination cycle of α-tubulin regulates microtubule functions. Perturbation of this cycle impairs mitosis, neural physiology, and cardiomyocyte contraction. The carboxypeptidases vasohibins 1 and 2 (VASH1 and VASH2), in complex with the small vasohibin-binding protein (SVBP), mediate α-tubulin detyrosination. These enzymes detyrosinate microtubules more efficiently than soluble αβ-tubulin heterodimers. The structural basis for this substrate preference is not understood. Using cryo-electron microscopy (cryo-EM), we have determined the structure of human VASH1-SVBP bound to microtubules. The acidic C-terminal tail of α-tubulin binds to a positively charged groove near the active site of VASH1. VASH1 forms multiple additional contacts with the globular domain of α-tubulin, including contacts with a second α-tubulin in an adjacent protofilament. Simultaneous engagement of two protofilaments by VASH1 can only occur within the microtubule lattice, but not with free αβ heterodimers. These lattice-specific interactions enable preferential detyrosination of microtubules by VASH1.

Indexed as

Carrier ProteinsCell Cycle ProteinsCryoelectron MicroscopyCrystallography, X-RayHeLa CellsHumansMicrotubulesProtein ConformationTubulinTyrosineCarrier ProteinsCell Cycle ProteinsSVBP protein, humanTubulinTyrosineVASH1 protein, humancryo-electron microscopydetyrosinationE. colimicrotubulemolecular biophysicsposttranslational modificationstructural biologyvasohibin

Identifiers

PMID32773040
PMCPMC7449697
OpenAlexW3048267638

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.