Evidence map›Paper›PMID 26929367›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Functional and topological diversity of LOV domain photoreceptors.

Spencer T Glantz, Eric J Carpenter, Michael Melkonian, Kevin H Gardner, Edward S Boyden, Gane Ka-Shu Wong, Brian Y Chow

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
29.5field-weighted citation impact, top 1% 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

75 citing papers in PubMed, 163 citations in OpenAlex.

  1. Review
  2. Structural Basis of a Novel Heme Binding Bacterial One-Component Switch.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Hydraulic Activation of the AsLOV2 Photoreceptor.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Article
  9. Xanthomonas campestris pv. campestris regulates virulence mechanisms by sensing blue light.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2025
    Article
  10. Review
  11. Protein design accelerates the development and application of optogenetic tools.Computational and structural biotechnology journal · 2025
    Review
  12. Article
  13. Article
  14. Review
  15. Rational Design of a Circularly Permuted Flavin-Based Fluorescent Protein.Chembiochem : a European journal of chemical biology · 2024
    Article
  16. Reengineering of a flavin-binding fluorescent protein using ProteinMPNN.Protein science : a publication of the Protein Society · 2024
    Article
  17. Article
  18. Review
  19. Article
  20. Article

15 more citing papers are in PubMed but not listed here.

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

7 authors at 6 institutions in 4 countries.

Spencer T GlantzDepartment of Bioengineering, University of Pennsylvania, Philadelphia, PA 19104;
Eric J CarpenterDepartment of Biological Sciences, University of Alberta, Edmonton, AB, Canada T6G 2E9;
Michael MelkonianInstitute of Botany, Cologne Biocenter, University of Cologne, 50674 Cologne, Germany;
Kevin H GardnerStructural Biology Initiative, CUNY Advanced Science Research Center, City College of New York, New York, NY 10031; Department of Chemistry and Biochemistry, City College of New York, New York, NY 10031; Biochemistry, Chemistry and Biology Programs, Graduate Center, The City University of New York, New York, NY 10031;ORCID http://orcid.org/0000-0002-8671-2556
Edward S BoydenThe Media Laboratory, Massachusetts Institute of Technology, Cambridge, MA 02139; Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139; Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139; McGovern Institute for Brain Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139;
Gane Ka-Shu WongDepartment of Biological Sciences, University of Alberta, Edmonton, AB, Canada T6G 2E9; Department of Medicine, University of Alberta, Edmonton, AB, Canada T6G 2E1; BGI-Shenzhen, Beishan Industrial Zone, Yantian District, Shenzhen 518083, China.
Brian Y ChowDepartment of Bioengineering, University of Pennsylvania, Philadelphia, PA 19104; bchow@seas.upenn.edu.
University of Pennsylvania · USBGI Group (China) · CNMcGovern Institute for Brain Research · USThe Graduate Center, CUNY · USUniversity of Alberta · CAUniversity of Cologne · DE

Funding

Novel Platforms for Systematic Optical Control of Complex Neural Circuits In VivoR01DA029639 · NIDA · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BOYDEN, EDWARD S. · 2010 to 2023
$6.7M
Summer Undergraduate Research Support - Ms. Anastasiia FisiukR01GM106239 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GARDNER, KEVIN H · 2013 to 2024
$4.5M
Redesigning General Anesthesia (Admin Supp)R01GM104948 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BOYDEN, EDWARD S., BROWN, EMERY N · 2012 to 2016
$4.4M
Novel Tools and Principles for Precisely Controlling Brain ActivityDP2OD002002 · OD · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BOYDEN, EDWARD S. · 2007 to 2007
$2.5M
CRCNS: Gamma Rhythms and Cell AssembliesR01NS067199 · NINDS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI KOPELL, NANCY · 2009 to 2013
$1.7M
Genetically-Encoded Tools for Manipulation of Ion Channel and Receptor FunctionsR01NS075421 · NINDS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BOYDEN, EDWARD S. · 2011 to 2014
$1.3M
Optogenetic control of attention through prefrontal synchronyRC1MH088182 · NIMH · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI DESIMONE, ROBERT · 2009 to 2010
$975k
Optogenetic Toolbox for Studying Regulators of G-Protein Signaling in AddictionR21DA040434 · NIDA · UNIVERSITY OF PENNSYLVANIA · PI CHOW, BRIAN Y · 2015 to 2016
$385k
NIDA NIH HHS 1R01DA029639NIDA NIH HHS 1R21 DA040434-01NIDA NIH HHS R01 DA029639NIDA NIH HHS R21 DA040434NIGMS NIH HHS 1R01GM104948NIGMS NIH HHS R01 GM104948NIGMS NIH HHS R01 GM106239NIH HHS 1DP2OD002002NIH HHS DP2 OD002002NIMH NIH HHS 1RC1MH088182NIMH NIH HHS RC1 MH088182NINDS NIH HHS 1R01NS067199NINDS NIH HHS 1R01NS075421NINDS NIH HHS R01 NS067199NINDS NIH HHS R01 NS075421
6 · The paper itself

Abstract

Light-oxygen-voltage sensitive (LOV) flavoproteins are ubiquitous photoreceptors that mediate responses to environmental cues. Photosensory inputs are transduced into signaling outputs via structural rearrangements in sensor domains that consequently modulate the activity of an effector domain or multidomain clusters. Establishing the diversity in effector function and sensor-effector topology will inform what signaling mechanisms govern light-responsive behaviors across multiple kingdoms of life and how these signals are transduced. Here, we report the bioinformatics identification of over 6,700 candidate LOV domains (including over 4,000 previously unidentified sequences from plants and protists), and insights from their annotations for ontological function and structural arrangements. Motif analysis identified the sensors from ∼42 million ORFs, with strong statistical separation from other flavoproteins and non-LOV members of the structurally related Per-aryl hydrocarbon receptor nuclear translocator (ARNT)-Sim family. Conserved-domain analysis determined putative light-regulated function and multidomain topologies. We found that for certain effectors, sensor-effector linker length is discretized based on both phylogeny and the preservation of α-helical heptad repeats within an extended coiled-coil linker structure. This finding suggests that preserving sensor-effector orientation is a key determinant of linker length, in addition to ancestry, in LOV signaling structure-function. We found a surprisingly high prevalence of effectors with functions previously thought to be rare among LOV proteins, such as regulators of G protein signaling, and discovered several previously unidentified effectors, such as lipases. This work highlights the value of applying genomic and transcriptomic technologies to diverse organisms to capture the structural and functional variation in photosensory proteins that are vastly important in adaptation, photobiology, and optogenetics.

Indexed as

Protein Structure, TertiaryAmino Acid MotifsAmino Acid SequenceAnimalsComputational BiologyConserved SequenceFlavoproteinsLightOpen Reading FramesPhotoreceptor Cells, InvertebratePhotoreceptors, MicrobialPhotoreceptors, PlantProgramming LanguagesStructure-Activity RelationshipFlavoproteinsPhotoreceptors, MicrobialPhotoreceptors, PlantflavoproteinsLOVoptogeneticsphotoreceptors

Identifiers

PMID26929367
PMCPMC4801262
OpenAlexW2292491794

What OpenQuestion holds

Textmetadata
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.