Evidence map›Paper›PMID 26755770›Full record

ArticleThe Journal of general physiology2016

Measuring distances between TRPV1 and the plasma membrane using a noncanonical amino acid and transition metal ion FRET.

William N Zagotta, Moshe T Gordon, Eric N Senning, Mika A Munari, Sharona E Gordon

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
6.3field-weighted citation impact, top 3% of its field
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

43 citing papers in PubMed, 81 citations in OpenAlex.

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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 at 1 institution in 1 country.

William N ZagottaDepartment of Physiology and Biophysics, University of Washington, Seattle, WA 98195 seg@uw.edu zagotta@uw.edu.
Moshe T GordonDepartment of Physiology and Biophysics, University of Washington, Seattle, WA 98195.
Eric N SenningDepartment of Physiology and Biophysics, University of Washington, Seattle, WA 98195.
Mika A MunariDepartment of Physiology and Biophysics, University of Washington, Seattle, WA 98195.
Sharona E GordonDepartment of Physiology and Biophysics, University of Washington, Seattle, WA 98195 seg@uw.edu zagotta@uw.edu.
University of Washington · US

Funding

Vector and Transgenic Mouse CoreP30DK017047 · NIDDK · UNIVERSITY OF WASHINGTON · PI Sakeneh Zraika · 1986 to 2026
$41.4M
Vision Research CoreP30EY001730 · NEI · UNIVERSITY OF WASHINGTON · PI MAUREEN E NEITZ · 1985 to 2026
$23.5M
EXPERIMENTAL PATHOLOGY OF CARDIOVASCULAR DISEASET32HL007312 · NHLBI · UNIVERSITY OF WASHINGTON · PI MAJESKY, MARK W., SCHWARTZ, STEPHEN MARK · 1985 to 2019
$11.8M
GATING MECHANISMS OF RETINAL ROD CGMP-ACTIVATED CHANNELSR01EY010329 · NEI · UNIVERSITY OF WASHINGTON · PI ZAGOTTA, WILLIAM N · 1994 to 2023
$7.7M
Inflammatory hyperalgesia mediated by TRPV1, the pepper spray receptor in the corR01EY017564 · NEI · UNIVERSITY OF WASHINGTON · PI GORDON, SHARONA E · 2006 to 2022
$6.5M
Regulation of KCNH ion channelsR01MH102378 · NIMH · UNIVERSITY OF WASHINGTON · PI ZAGOTTA, WILLIAM N · 2014 to 2018
$1.9M
Supplement to Multimodal Gating Mechanisms of TRPV1 Ion ChannelsR01GM125351 · NIGMS · UNIVERSITY OF WASHINGTON · PI GORDON, SHARONA E · 2018 to 2021
$1.8M
Mechanisms of TRPV1 Channel RegulationR01GM100718 · NIGMS · UNIVERSITY OF WASHINGTON · PI GORDON, SHARONA E, ZAGOTTA, WILLIAM N · 2012 to 2015
$1.5M
Electrophysiology-Optical Workstation for Ion Channel BiophysicsS10RR025429 · NCRR · UNIVERSITY OF WASHINGTON · PI GORDON, SHARONA E · 2009 to 2009
$499k
NCRR NIH HHS S10 RR025429NCRR NIH HHS S10RR025429NEI NIH HHS P30 EY001730NEI NIH HHS P30EY001730NEI NIH HHS R01 EY010329NEI NIH HHS R01EY010329NEI NIH HHS R01 EY017564NEI NIH HHS R01EY017564NHLBI NIH HHS T32 HL007312NHLBI NIH HHS T32HL007312NIDDK NIH HHS P30 DK017047NIDDK NIH HHS P30DK017047NIGMS NIH HHS R01 GM100718NIGMS NIH HHS R01GM100718NIGMS NIH HHS R01 GM125351NIMH NIH HHS R01 MH102378NIMH NIH HHS R01MH102378
6 · The paper itself

Abstract

Despite recent advances, the structure and dynamics of membrane proteins in cell membranes remain elusive. We implemented transition metal ion fluorescence resonance energy transfer (tmFRET) to measure distances between sites on the N-terminal ankyrin repeat domains (ARDs) of the pain-transducing ion channel TRPV1 and the intracellular surface of the plasma membrane. To preserve the native context, we used unroofed cells, and to specifically label sites in TRPV1, we incorporated a fluorescent, noncanonical amino acid, L-ANAP. A metal chelating lipid was used to decorate the plasma membrane with high-density/high-affinity metal-binding sites. The fluorescence resonance energy transfer (FRET) efficiencies between L-ANAP in TRPV1 and Co(2+) bound to the plasma membrane were consistent with the arrangement of the ARDs in recent cryoelectron microscopy structures of TRPV1. No change in tmFRET was observed with the TRPV1 agonist capsaicin. These results demonstrate the power of tmFRET for measuring structure and rearrangements of membrane proteins relative to the cell membrane.

Indexed as

Amino AcidsBinding SitesCapsaicinCell MembraneFluorescence Resonance Energy TransferFluorescent DyesHEK293 CellsHumansMembrane ProteinsMetalsProtein Structure, TertiaryTRPV Cation ChannelsAmino AcidsCapsaicinFluorescent DyesMembrane ProteinsMetalsTRPV1 protein, humanTRPV Cation Channels

Identifiers

PMID26755770
PMCPMC4727949
OpenAlexW2258885744

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.