Evidence map›Paper›PMID 37016670›Full record

ArticlebioRxiv : the preprint server for biology2023

A structural vista of phosducin-like PhLP2A-chaperonin TRiC cooperation during the ATP-driven folding cycle.

Junsun Park, Hyunmin Kim, Daniel Gestaut, Seyeon Lim, Alexander Leitner, Judith Frydman, Soung-Hun Roh

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
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. Not yet cited in PubMed.

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

0 citing papers in PubMed, 6 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 3 countries.

Junsun ParkSchool of Biological Sciences, Institute of Molecular Biology and Genetics, Seoul National University, Seoul, South Korea.
Hyunmin KimSchool of Biological Sciences, Institute of Molecular Biology and Genetics, Seoul National University, Seoul, South Korea.
Daniel GestautDept of Biology, Stanford University, Stanford, CA 94305, USA.
Seyeon LimSchool of Biological Sciences, Institute of Molecular Biology and Genetics, Seoul National University, Seoul, South Korea.
Alexander LeitnerInstitute of Molecular Systems Biology, Dept of Biology, ETH Zurich, 8093 Zurich, Switzerland.
Judith FrydmanDept of Genetics, Stanford University, Stanford, CA 94305, USA.
Soung-Hun RohSchool of Biological Sciences, Institute of Molecular Biology and Genetics, Seoul National University, Seoul, South Korea.
Seoul National University · KRStanford University · USETH Zurich · CH

Funding

Mechanism of the Eukaryotic Chaperonin TRiC/CCTR01GM074074 · NIGMS · STANFORD UNIVERSITY · PI FRYDMAN, JUDITH · 2005 to 2024
$6.8M
NIGMS NIH HHS R01 GM074074
6 · The paper itself

Abstract

Proper cellular proteostasis, essential for viability, requires a network of chaperones and cochaperones. ATP-dependent chaperonin TRiC/CCT partners with cochaperones prefoldin (PFD) and phosducin-like proteins (PhLPs) to facilitate the folding of essential eukaryotic proteins. Using cryoEM and biochemical analyses, we determine the ATP-driven cycle of TRiC-PFD-PhLP2A interaction. In the open TRiC state, PhLP2A binds to the chamber's equator while its N-terminal H3-domain binds to the apical domains of CCT3/4, thereby displacing PFD from TRiC. ATP-induced TRiC closure rearranges the contacts of PhLP2A domains within the closed chamber. In the presence of substrate, actin and PhLP2A segregate into opposing chambers, each binding to the positively charged inner surfaces formed by CCT1/3/6/8. Notably, actin induces a conformational change in PhLP2A, causing its N-terminal helices to extend across the inter-ring interface to directly contact a hydrophobic groove in actin. Our findings reveal an ATP-driven PhLP2A structural rearrangement cycle within the TRiC chamber to facilitate folding.

Indexed as

ActinChaperonin TRiC/CCTCochaperoneCryoEMPhLP2APhosducin-like protein (PhLP)PrefoldinProtein folding

Identifiers

PMID37016670
PMCPMC10071816
OpenAlexW4360979534

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.