Evidence map›Paper›PMID 38850532›Full record

ArticleCell reports2024

Tentonin 3 is a pore-forming subunit of a slow inactivation mechanosensitive channel.

Sungmin Pak, Hyunil Ryu, Sujin Lim, Thien-Luan Nguyen, Sungwook Yang, Sumin Kang, Yeon Gyu Yu, Junhyuk Woo, Chanjin Kim, Cristina Fenollar-Ferrer and 6 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
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

16 authors.

Sungmin PakBrain Science Institute, Korea Institute of Science and Technology (KIST), Seoul 02792, Korea; College of Pharmacy, Seoul National University, Seoul 08826, Korea.
Hyunil RyuBrain Science Institute, Korea Institute of Science and Technology (KIST), Seoul 02792, Korea.
Sujin LimBrain Science Institute, Korea Institute of Science and Technology (KIST), Seoul 02792, Korea; Department of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, Seoul National University, Seoul 08826, Korea.
Thien-Luan NguyenBrain Science Institute, Korea Institute of Science and Technology (KIST), Seoul 02792, Korea; College of Pharmacy, Seoul National University, Seoul 08826, Korea.
Sungwook YangArtificial Intelligence and Robotics Institute, KIST, Seoul 02792, Korea.
Sumin KangDepartment of Chemistry, Kookmin University, Seoul 02707, Korea.
Yeon Gyu YuDepartment of Chemistry, Kookmin University, Seoul 02707, Korea.
Junhyuk WooBrain Science Institute, Korea Institute of Science and Technology (KIST), Seoul 02792, Korea.
Chanjin KimBrain Science Institute, Korea Institute of Science and Technology (KIST), Seoul 02792, Korea.
Cristina Fenollar-FerrerStiles-Nicholson Brain Institute at Florida Atlantic University, Jupiter, FL 33458, USA; Laboratory of Molecular Genetics, NIDCD, NIH, Bethesda, MD 20892, USA.
John N WoodMolecular Nociception Group, Wolfson Institute for Biomedical Research, University College London, London WC1E 6BT, UK.
Mi-Ock LeeCollege of Pharmacy, Seoul National University, Seoul 08826, Korea.
Gyu-Sang HongBrain Science Institute, Korea Institute of Science and Technology (KIST), Seoul 02792, Korea; Division of Bio-Medical Science & Technology, KIST School, University of Science and Technology, Seoul 02792, Korea; Department of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, Seoul National University, Seoul 08826, Korea. Electronic address: gshong@kist.re.kr.
Kyungreem HanBrain Science Institute, Korea Institute of Science and Technology (KIST), Seoul 02792, Korea; Division of Bio-Medical Science & Technology, KIST School, University of Science and Technology, Seoul 02792, Korea. Electronic address: khan@kist.re.kr.
Tae Song KimBrain Science Institute, Korea Institute of Science and Technology (KIST), Seoul 02792, Korea. Electronic address: tskim@kist.re.kr.
Uhtaek OhBrain Science Institute, Korea Institute of Science and Technology (KIST), Seoul 02792, Korea; Department of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, Seoul National University, Seoul 08826, Korea. Electronic address: utoh@kist.re.kr.

Funding

Identification of Genes Causing Syndromic And Nonsyndromic Hearing ImpairmentZ01DC000039 · NIDCD · NATIONAL INSTITUTE ON DEAFNESS AND OTHER COMMUNICATION DISORDERS · PI FRIEDMAN, THOMAS BAER · 1997 to 2008
$7.2M
SPEECH AND HEARING SCIENCEST32DC000039 · NIDCD · CUNY GRADUATE SCH AND UNIV CTR · PI SCHWARTZ, RICHARD G · 1992 to 2002
$429k
Intramural NIH HHS Z01 DC000039NIDCD NIH HHS T32 DC000039
6 · The paper itself

Abstract

Mechanically activating (MA) channels transduce numerous physiological functions. Tentonin 3/TMEM150C (TTN3) confers MA currents with slow inactivation kinetics in somato- and barosensory neurons. However, questions were raised about its role as a Piezo1 regulator and its potential as a channel pore. Here, we demonstrate that purified TTN3 proteins incorporated into the lipid bilayer displayed spontaneous and pressure-sensitive channel currents. These MA currents were conserved across vertebrates and differ from Piezo1 in activation threshold and pharmacological response. Deep neural network structure prediction programs coupled with mutagenetic analysis predicted a rectangular-shaped, tetrameric structure with six transmembrane helices and a pore at the inter-subunit center. The putative pore aligned with two helices of each subunit and had constriction sites whose mutations changed the MA currents. These findings suggest that TTN3 is a pore-forming subunit of a distinct slow inactivation MA channel, potentially possessing a tetrameric structure.

Indexed as

Ion ChannelsAmino Acid SequenceAnimalsHEK293 CellsHumansLipid BilayersMechanotransduction, CellularMembrane ProteinsMiceMutationProtein SubunitsIon ChannelsLipid BilayersMembrane ProteinsProtein SubunitsTMEM150C protein, humanCP: Molecular biology

Identifiers

PMID38850532
PMCPMC11310380

What OpenQuestion holds

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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.