Evidence map›Paper›PMID 37805833›Full record

ArticleProtein science : a publication of the Protein Society2023

Photomodulation of the ASIC1a acidic pocket destabilizes the open state.

Matthew L Rook, Tyler W McCullock, Tyler Couch, John D Lueck, David M MacLean

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Mechanism of acid-sensing ion channel modulation by Hi1a.The Journal of general physiology · 2024
    Article
  2. Review
  3. Review
  4. A conserved peptide-binding pocket in HyNaC/ASIC ion channels.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Photomodulation of the ASIC1a acidic pocket destabilizes the open state.Protein science : a publication of the Protein Society · 2023
    Article
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

5 authors.

Matthew L RookDepartment of Pharmacology and Physiology, School of Medicine and Dentistry, University of Rochester, Rochester, New York, USA.
Tyler W McCullockDepartment of Pharmacology and Physiology, School of Medicine and Dentistry, University of Rochester, Rochester, New York, USA.
Tyler CouchDepartment of Pharmacology and Physiology, School of Medicine and Dentistry, University of Rochester, Rochester, New York, USA.
John D LueckDepartment of Pharmacology and Physiology, School of Medicine and Dentistry, University of Rochester, Rochester, New York, USA.
David M MacLeanDepartment of Pharmacology and Physiology, School of Medicine and Dentistry, University of Rochester, Rochester, New York, USA.ORCID 0000-0001-8294-6075

Funding

The GCE4All Center: Unleashing the Potential of Genetic Code Expansion for Biomedical ResearchRM1GM144227 · NIGMS · OREGON STATE UNIVERSITY · PI RYAN A MEHL · 2022 to 2026
$6.2M
Training in Cellular, Biochemical and Molecular SciencesT32GM068411 · NIGMS · UNIVERSITY OF ROCHESTER · PI MAQUAT, LYNNE E · 2005 to 2019
$3.9M
Acid-Sensing Ion Channel gating: Conformations and ConsequencesR35GM137951 · NIGMS · UNIVERSITY OF ROCHESTER · PI David Malcolm MacLean · 2020 to 2026
$2.8M
Optical interrogation of acid-sensing ion channel activation and desensitization through genetic code expansionF31NS120445 · NINDS · UNIVERSITY OF ROCHESTER · PI ROOK, MATTHEW L · 2021 to 2021
$46k
NIGMS NIH HHS R35 GM137951NIGMS NIH HHS R35GM137951NIGMS NIH HHS RM1 GM144227NIGMS NIH HHS RM1-GM144227NIGMS NIH HHS T32 GM068411NIGMS NIH HHS T32GM068411NINDS NIH HHS F31 NS120445NINDS NIH HHS F31NS120445
6 · The paper itself

Abstract

Acid-sensing ion channels (ASICs) are important players in detecting extracellular acidification throughout the brain and body. ASICs have large extracellular domains containing two regions replete with acidic residues: the acidic pocket, and the palm domain. In the resting state, the acidic pocket is in an expanded conformation but collapses in low pH conditions as the acidic side chains are neutralized. Thus, extracellular acidification has been hypothesized to collapse the acidic pocket that, in turn, ultimately drives channel activation. However, several observations run counter to this idea. To explore how collapse or mobility of the acidic pocket is linked to channel gating, we employed two distinct tools. First, we incorporated the photocrosslinkable noncanonical amino acids (ncAAs) 4-azido-L-phenylalanine (AzF) or 4-benzoyl-L-phenylalanine (BzF) into several positions in the acidic pocket. At both E315 and Y318, AzF incorporation followed by UV irradiation led to right shifts in pH response curves and accelerations of desensitization and deactivation, consistent with restrictions of acidic pocket mobility destabilizing the open state. Second, we reasoned that because Cl

Indexed as

Acid Sensing Ion ChannelsHydrogen-Ion ConcentrationMolecular ConformationAcid Sensing Ion Channelsacidic pocketacid-sensing ion channelsASICsgatinggenetic code expansionphotomodulation

Identifiers

PMID37805833
PMCPMC10599103

What OpenQuestion holds

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Registered trials

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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.