Evidence map›Paper›PMID 27402735›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study.

Rui Huang, Zev A Ripstein, Rafal Augustyniak, Michal Lazniewski, Krzysztof Ginalski, Lewis E Kay, John L Rubinstein

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
27.3field-weighted citation impact, top 1% 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

33 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. APlants (Basel, Switzerland) · 2025
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  6. Dissecting the role of interprotomer cooperativity in the activation of oligomeric high-temperature requirement A2 protein.Proceedings of the National Academy of Sciences of the United States of America · 2021
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  7. Review
  8. Protein Dynamics revealed by NMR Relaxation Methods.Emerging topics in life sciences · 2020
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  11. Direct visualization of degradation microcompartments at the ER membrane.Proceedings of the National Academy of Sciences of the United States of America · 2020
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  14. Review
  15. Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase.Cold Spring Harbor perspectives in biology · 2019
    Review
  16. Article
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  18. Article
  19. Reversible inhibition of the ClpP protease via an N-terminal conformational switch.Proceedings of the National Academy of Sciences of the United States of America · 2018
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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

7 authors at 3 institutions in 2 countries.

Rui HuangDepartment of Molecular Genetics, University of Toronto, Toronto, ON, Canada M5S 1A8; Department of Chemistry, University of Toronto, Toronto, ON, Canada M5S 3H6; Department of Biochemistry, University of Toronto, Toronto, ON, Canada M5S 1A8;
Zev A RipsteinDepartment of Biochemistry, University of Toronto, Toronto, ON, Canada M5S 1A8; The Hospital for Sick Children Research Institute, Toronto, ON, Canada M5G 0A4;
Rafal AugustyniakDepartment of Molecular Genetics, University of Toronto, Toronto, ON, Canada M5S 1A8; Department of Chemistry, University of Toronto, Toronto, ON, Canada M5S 3H6; Department of Biochemistry, University of Toronto, Toronto, ON, Canada M5S 1A8;
Michal LazniewskiLaboratory of Bioinformatics and Systems Biology, Centre of New Technologies, University of Warsaw, 02-089 Warsaw, Poland; Department of Physical Chemistry, Faculty of Pharmacy, Medical University of Warsaw, 02-097 Warsaw, Poland;
Krzysztof GinalskiLaboratory of Bioinformatics and Systems Biology, Centre of New Technologies, University of Warsaw, 02-089 Warsaw, Poland;
Lewis E KayDepartment of Molecular Genetics, University of Toronto, Toronto, ON, Canada M5S 1A8; Department of Chemistry, University of Toronto, Toronto, ON, Canada M5S 3H6; Department of Biochemistry, University of Toronto, Toronto, ON, Canada M5S 1A8; The Hospital for Sick Children Research Institute, Toronto, ON, Canada M5G 0A4; kay@pound.med.utoronto.ca john.rubinstein@utoronto.ca.
John L RubinsteinDepartment of Biochemistry, University of Toronto, Toronto, ON, Canada M5S 1A8; The Hospital for Sick Children Research Institute, Toronto, ON, Canada M5G 0A4; Department of Medical Biophysics, University of Toronto, Toronto, ON, Canada M5G 1L7 kay@pound.med.utoronto.ca john.rubinstein@utoronto.ca.
University of Toronto · CAUniversity of Warsaw · PLHospital for Sick Children · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The AAA+ (ATPases associated with a variety of cellular activities) enzymes play critical roles in a variety of homeostatic processes in all kingdoms of life. Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), the archaeal homolog of the ubiquitous AAA+ protein Cdc48/p97, functions in concert with the 20S proteasome by unfolding substrates and passing them on for degradation. Here, we present electron cryomicroscopy (cryo-EM) maps showing that VAT undergoes large conformational rearrangements during its ATP hydrolysis cycle that differ dramatically from the conformational states observed for Cdc48/p97. We validate key features of the model with biochemical and solution methyl-transverse relaxation optimized spectroscopY (TROSY) NMR experiments and suggest a mechanism for coupling the energy of nucleotide hydrolysis to substrate unfolding. These findings illustrate the unique complementarity between cryo-EM and solution NMR for studies of molecular machines, showing that the structural properties of VAT, as well as the population distributions of conformers, are similar in the frozen specimens used for cryo-EM and in the solution phase where NMR spectra are recorded.

Indexed as

Archaeal ProteinsCryoelectron MicroscopyNuclear Magnetic Resonance, BiomolecularProtein ConformationThermoplasmaValosin Containing ProteinArchaeal ProteinsValosin Containing Proteinvat protein, Thermoplasma acidophilumcryo-EMmethyl-TROSY NMRproteasomeprotein dynamicsVAT

Identifiers

PMID27402735
PMCPMC4961139
OpenAlexW2466683540

What OpenQuestion holds

Textmetadata
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.