Evidence map›Paper›PMID 38654823›Full record

ArticlebioRxiv : the preprint server for biology2023

Visualization of the Cdc48 AAA+ ATPase protein unfolding pathway.

Ian Cooney, Heidi L Schubert, Karina Cedeno, Hsien-Jung L Lin, John C Price, Christopher P Hill, Peter S Shen

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Upregulation of Piezo2 and increased extracellular matrix protein in diabetic kidney disease mice.Hypertension research : official journal of the Japanese Society of Hypertension · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Ian CooneyDepartment of Biochemistry, 15 N. Medical Drive East, University of Utah, Salt Lake City, UT, 84112, USA.
Heidi L SchubertDepartment of Biochemistry, 15 N. Medical Drive East, University of Utah, Salt Lake City, UT, 84112, USA.
Karina CedenoDepartment of Biochemistry, 15 N. Medical Drive East, University of Utah, Salt Lake City, UT, 84112, USA.
Hsien-Jung L LinDepartment of Chemistry and Biochemistry, C100 BNSN, Brigham Young University, Provo, UT, 84602, USA.
John C PriceDepartment of Chemistry and Biochemistry, C100 BNSN, Brigham Young University, Provo, UT, 84602, USA.
Christopher P HillDepartment of Biochemistry, 15 N. Medical Drive East, University of Utah, Salt Lake City, UT, 84112, USA.
Peter S ShenDepartment of Biochemistry, 15 N. Medical Drive East, University of Utah, Salt Lake City, UT, 84112, USA.ORCID 0000-0002-6256-6910

Funding

CHEETAH Center for the Structural Biology of HIV Infection, Restriction, and Viral DynamicsU54AI170856 · NIAID · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Pamela J Bjorkman · 2022 to 2026
$34.4M
ESCRT-III and MIT Protein Complexes in CytokinesisR01GM112080 · NIGMS · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI CHRISTOPHER P. HILL, WESLEY I. SUNDQUIST · 2014 to 2026
$4.1M
Visualizing the Mechanisms of Protein Quality ControlR35GM133772 · NIGMS · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Peter Shen · 2019 to 2026
$3.4M
Biochemical Consequences of Regiospecific Metabolic Bias in the BrainR01AG066874 · NIA · BRIGHAM YOUNG UNIVERSITY · PI PRICE, JOHN C. · 2020 to 2024
$3.0M
Resolving the mechanism of cofactor and substrate interactions with Cdc48F31CA254427 · NCI · UNIVERSITY OF UTAH · PI COONEY, IAN · 2020 to 2022
$111k
NCI NIH HHS F31 CA254427NIAID NIH HHS U54 AI170856NIA NIH HHS R01 AG066874NIGMS NIH HHS R01 GM112080NIGMS NIH HHS R35 GM133772
6 · The paper itself

Abstract

The Cdc48 AAA+ ATPase is an abundant and essential enzyme that unfolds substrates in multiple protein quality control pathways. The enzyme includes two conserved AAA+ ATPase cassettes, D1 and D2, that assemble as hexameric rings with D1 stacked above D2. Here, we report an ensemble of structures of Cdc48 affinity purified from lysate in complex with the adaptor Shp1 in the act of unfolding substrate. Our analysis reveals a continuum of structural snapshots that spans the entire translocation cycle. These data reveal new elements of Shp1-Cdc48 binding and support a "hand-over-hand" mechanism in which the sequential movement of individual subunits is closely coordinated. D1 hydrolyzes ATP and disengages from substrate prior to D2, while D2 rebinds ATP and re-engages with substrate prior to D1, thereby explaining the dominant role played by D2 in substrate translocation/unfolding.

Identifiers

PMID38654823
PMCPMC11037871

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.