Evidence map›Paper›PMID 33990694›Full record

ArticleCommunications biology2021

Time-resolved spectroscopic and electrophysiological data reveal insights in the gating mechanism of anion channelrhodopsin.

Max-Aylmer Dreier, Philipp Althoff, Mohamad Javad Norahan, Stefan Alexander Tennigkeit, Samir F El-Mashtoly, Mathias Lübben, Carsten Kötting, Till Rudack, Klaus Gerwert

Abstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Apusomonad rhodopsins: A new family of ultraviolet to blue light-absorbing rhodopsin channels.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

9 authors.

Max-Aylmer DreierBiospectroscopy, Center for Protein Diagnostics (PRODI), Ruhr University Bochum, Bochum, Germany.ORCID http://orcid.org/0000-0003-0056-014X
Philipp AlthoffBiospectroscopy, Center for Protein Diagnostics (PRODI), Ruhr University Bochum, Bochum, Germany.
Mohamad Javad NorahanBiospectroscopy, Center for Protein Diagnostics (PRODI), Ruhr University Bochum, Bochum, Germany.
Stefan Alexander TennigkeitBiospectroscopy, Center for Protein Diagnostics (PRODI), Ruhr University Bochum, Bochum, Germany.
Samir F El-MashtolyBiospectroscopy, Center for Protein Diagnostics (PRODI), Ruhr University Bochum, Bochum, Germany.ORCID http://orcid.org/0000-0001-6087-8817
Mathias LübbenBiospectroscopy, Center for Protein Diagnostics (PRODI), Ruhr University Bochum, Bochum, Germany.
Carsten KöttingBiospectroscopy, Center for Protein Diagnostics (PRODI), Ruhr University Bochum, Bochum, Germany.ORCID http://orcid.org/0000-0002-3599-9657
Till RudackBiospectroscopy, Center for Protein Diagnostics (PRODI), Ruhr University Bochum, Bochum, Germany. till.rudack@rub.de.ORCID http://orcid.org/0000-0003-2693-9561
Klaus GerwertBiospectroscopy, Center for Protein Diagnostics (PRODI), Ruhr University Bochum, Bochum, Germany. klaus.gerwert@rub.de.ORCID http://orcid.org/0000-0001-8759-5964

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Channelrhodopsins are widely used in optogenetic applications. High photocurrents and low current inactivation levels are desirable. Two parallel photocycles evoked by different retinal conformations cause cation-conducting channelrhodopsin-2 (CrChR2) inactivation: one with efficient conductivity; one with low conductivity. Given the longer half-life of the low conducting photocycle intermediates, which accumulate under continuous illumination, resulting in a largely reduced photocurrent. Here, we demonstrate that for channelrhodopsin-1 of the cryptophyte Guillardia theta (GtACR1), the highly conducting C = N-anti-photocycle was the sole operating cycle using time-resolved step-scan FTIR spectroscopy. The correlation between our spectroscopic measurements and previously reported electrophysiological data provides insights into molecular gating mechanisms and their role in the characteristic high photocurrents. The mechanistic importance of the central constriction site amino acid Glu-68 is also shown. We propose that canceling out the poorly conducting photocycle avoids the inactivation observed in CrChR2, and anticipate that this discovery will advance the development of optimized optogenetic tools.

Indexed as

Electrophysiological PhenomenaIon Channel GatingAnionsChannelrhodopsinsCryptophytaLightOptogeneticsSpectrophotometryAnionsChannelrhodopsins

Identifiers

PMID33990694
PMCPMC8121809

What OpenQuestion holds

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LicenceCC BY
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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.