Evidence map›Paper›PMID 37398045›Full record

ArticlebioRxiv : the preprint server for biology2024

Complexes of vertebrate TMC1/2 and CIB2/3 proteins form hair-cell mechanotransduction cation channels.

Arnaud P J Giese, Wei-Hsiang Weng, Katie S Kindt, Hui Ho Vanessa Chang, Jonathan S Montgomery, Evan M Ratzan, Alisha J Beirl, Roberto Aponte Rivera, Jeffrey M Lotthammer, Sanket Walujkar and 7 more

Open access · greenAbstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2024. 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, 10 citations in OpenAlex.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

17 authors at 6 institutions in 2 countries.

Arnaud P J GieseDepartment of Otorhinolaryngology - Head & Neck Surgery, University of Maryland School of Medicine, Baltimore, MD, USA.
Wei-Hsiang WengDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
Katie S KindtSection on Sensory Cell Development and Function, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda, MD, USA.
Hui Ho Vanessa ChangDepartment of Physiology, McGill University, Montreal, QC, Canada.
Jonathan S MontgomeryDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
Evan M RatzanDepartments of Otolaryngology and Neurology, F.M. Kirby Neurobiology Center, Boston Children's Hospital, Harvard Medical School, Boston, MA, USA.
Alisha J BeirlSection on Sensory Cell Development and Function, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda, MD, USA.
Roberto Aponte RiveraSection on Sensory Cell Development and Function, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda, MD, USA.
Jeffrey M LotthammerDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
Sanket WalujkarDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
Mark P FosterDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.ORCID 0000-0001-9645-7491
Omid A ZobeiriDepartment of Biomedical Engineering, McGill University, Montreal, QC, Canada.
Jeffrey R HoltDepartments of Otolaryngology and Neurology, F.M. Kirby Neurobiology Center, Boston Children's Hospital, Harvard Medical School, Boston, MA, USA.
Saima RiazuddinDepartment of Otorhinolaryngology - Head & Neck Surgery, University of Maryland School of Medicine, Baltimore, MD, USA.
Kathleen E CullenDepartments of Biomedical Engineering, Neuroscience, and Otolaryngology and Head and Neck Surgery, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Marcos SotomayorDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
Zubair M AhmedDepartment of Otorhinolaryngology - Head & Neck Surgery, University of Maryland School of Medicine, Baltimore, MD, USA.
The Ohio State University · USNational Institutes of Health · USUniversity of Maryland, Baltimore · USBoston Children's Hospital · USMcGill University · CAJohns Hopkins University · US

Funding

In vivo investigation of sensory hair cell function and developmentZIADC000085 · NIDCD · NATIONAL INSTITUTE ON DEAFNESS AND OTHER COMMUNICATION DISORDERS · PI KINDT, KATIE · 2014 to 2025
$21.4M
The Physiology of Vestibular CompensationR01DC002390 · NIDCD · JOHNS HOPKINS UNIVERSITY · PI Kathleen E Cullen · 1995 to 2026
$10.7M
Genetic Analysis and Manipulation Core (GAEC)P50HD105351 · NICHD · BOSTON CHILDREN'S HOSPITAL · PI SCOTT Loren POMEROY, MUSTAFA SAHIN · 2021 to 2026
$9.4M
Usher Proteins in the Inner Ear Structure and FunctionR01DC012564 · NIDCD · UNIVERSITY OF MARYLAND BALTIMORE · PI Zubair M. Ahmed, Gregory I Frolenkov · 2013 to 2026
$7.0M
Neural Computations Underlying Cancellation of the Vestibular Consequences of Voluntary MovementR01DC018061 · NIDCD · JOHNS HOPKINS UNIVERSITY · PI Kathleen E Cullen · 2019 to 2026
$4.0M
Mechanism and Functional Significance of Polarity Reversal in Mechanosensory OrgansR01DC018304 · NIDCD · JACKSON LABORATORY · PI CULLEN, KATHLEEN E, EATOCK, RUTH ANNE · 2020 to 2024
$3.5M
Nanomechanics of Inner Ear Hair Cell TransductionR01DC015271 · NIDCD · UNIVERSITY OF CHICAGO · PI Marcos Sotomayor · 2016 to 2026
$3.5M
A Neural Systems Approach to Understanding the Dynamic Computations Underlying our Sense of DirectionUF1NS111695 · NINDS · DARTMOUTH COLLEGE · PI TAUBE, JEFFREY STEVEN, VAN DER MEER, MATTHIJS · 2019 to 2019
$3.0M
Molecular biophysics predoctoral training at the Ohio State UniversityT32GM144293 · NIGMS · OHIO STATE UNIVERSITY · PI CHARLES E BELL, Ralf A Bundschuh · 2022 to 2026
$1.1M
Intramural NIH HHS ZIA DC000085NICHD NIH HHS P50 HD105351NIDCD NIH HHS R01 DC002390NIDCD NIH HHS R01 DC012564NIDCD NIH HHS R01 DC015271NIDCD NIH HHS R01 DC018061NIDCD NIH HHS R01 DC018304NIGMS NIH HHS T32 GM144293NINDS NIH HHS UF1 NS111695
6 · The paper itself

Abstract

Calcium and integrin-binding protein 2 (CIB2) and CIB3 bind to transmembrane channel-like 1 (TMC1) and TMC2, the pore-forming subunits of the inner-ear mechano-electrical transduction (MET) apparatus. These interactions have been proposed to be functionally relevant across mechanosensory organs and vertebrate species. Here we show that both CIB2 and CIB3 can form heteromeric complexes with TMC1 and TMC2 and are integral for MET function in mouse cochlea and vestibular end organs as well as in zebrafish inner ear and lateral line. Our AlphaFold 2 models suggest that vertebrate CIB proteins can simultaneously interact with at least two cytoplasmic domains of TMC1 and TMC2 as validated using nuclear magnetic resonance spectroscopy of TMC1 fragments interacting with CIB2 and CIB3. Molecular dynamics simulations of TMC1/2 complexes with CIB2/3 predict that TMCs are structurally stabilized by CIB proteins to form cation channels. Overall, our work demonstrates that intact CIB2/3 and TMC1/2 complexes are integral to hair-cell MET function in vertebrate mechanosensory epithelia.

Indexed as

CIB2CIB3mechanotransductionTMC1TMC2Vestibular hair cells

Identifiers

PMID37398045
PMCPMC10312449
OpenAlexW4378837212

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.