Evidence map›Paper›PMID 33781746›Full record

ReviewThe Journal of biological chemistry

Lighting the way: Recent insights into the structure and regulation of phototropin blue light receptors.

Jaynee E Hart, Kevin H Gardner

Open access · goldAbstract readReview
In one paragraph

Review in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
6.0field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025
    Review
  10. Machine Learning Approach to Vertical Energy Gap in Redox Processes.Journal of chemical theory and computation · 2024
    Article
  11. Light Control in Microbial Systems.International journal of molecular sciences · 2024
    Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Small RNA-mediated silencing of phototropin suppresses the induction of photoprotection in the green algaProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Article
  19. Review
  20. Review
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

2 authors at 1 institution in 1 country.

Jaynee E HartStructural Biology Initiative, CUNY Advanced Science Research Center, New York, New York, USA.
Kevin H GardnerStructural Biology Initiative, CUNY Advanced Science Research Center, New York, New York, USA; Department of Chemistry and Biochemistry, City College of New York, New York, USA; PhD Programs in Biochemistry, Chemistry, and Biology, Graduate Center, City University of New York, New York, USA. Electronic address: kgardner@gc.cuny.edu.
The Graduate Center, CUNY · US

Funding

Summer Undergraduate Research Support - Ms. Anastasiia FisiukR01GM106239 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GARDNER, KEVIN H · 2013 to 2024
$4.5M
NIGMS NIH HHS R01 GM106239
6 · The paper itself

Abstract

The phototropins (phots) are light-activated kinases that are critical for plant physiology and the many diverse optogenetic tools that they have inspired. Phototropins combine two blue-light-sensing Light-Oxygen-Voltage (LOV) domains (LOV1 and LOV2) and a C-terminal serine/threonine kinase domain, using the LOV domains to control the catalytic activity of the kinase. While much is known about the structure and photochemistry of the light-perceiving LOV domains, particularly in how activation of the LOV2 domain triggers the unfolding of alpha helices that communicate the light signal to the kinase domain, many questions about phot structure and mechanism remain. Recent studies have made progress addressing these questions by utilizing small-angle X-ray scattering (SAXS) and other biophysical approaches to study multidomain phots from Chlamydomonas and Arabidopsis, leading to models where the domains have an extended linear arrangement, with the regulatory LOV2 domain contacting the kinase domain N-lobe. We discuss this and other advances that have improved structural and mechanistic understanding of phot regulation in this review, along with the challenges that will have to be overcome to obtain high-resolution structural information on these exciting photoreceptors. Such information will be essential to advancing fundamental understanding of plant physiology while enabling engineering efforts at both the whole plant and molecular levels.

Indexed as

LightArabidopsisChlamydomonas reinhardtiiCrystallography, X-RayModels, MolecularPhototropinsPlant ProteinsProtein ConformationPhototropinsPlant Proteinsallosteric regulationoptogeneticsphototransductionprotein engineeringprotein kinasesignaling

Identifiers

PMID33781746
PMCPMC8086140
OpenAlexW3147319126

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.