Evidence map›Paper›PMID 42402218›Full record

ArticleThe Plant journal : for cell and molecular biology2026

Hypsochromic shift in phytochrome C Pr absorption complements phytochrome B-mediated inhibition of hypocotyl elongation.

Shizue Yoshihara, Koji Okajima, Satoru Tokutomi

Abstract read
In one paragraph

Article in The Plant journal : for cell and molecular biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Shizue YoshiharaGraduate School of Science, Osaka Metropolitan University, Sakai, Osaka, Japan.ORCID https://orcid.org/0000-0001-6412-9231
Koji OkajimaDepartment of Physics, Faculty of Science and Technology, Keio University, Yokohama, Kanagawa, Japan.
Satoru TokutomiGraduate School of Science, Osaka Prefecture University, Sakai, Osaka, Japan.

Funding

Japan Society for the Promotion of Science 23657105Japan Society for the Promotion of Science 6K14830Research Support Program for Enhancing Capability and Techniques From Osaka Prefecture University
6 · The paper itself

Abstract

Phytochromes are red/far-red light photoreceptors that regulate diverse aspects of plant photomorphogenesis. Among angiosperm phytochromes, phytochrome C (phyC) is the least well characterized, despite its conservation across monocots and dicots. Previous studies have suggested that phyC exhibits absorption properties distinct from those of phyA and phyB, but the physiological significance of these differences has remained unclear. Here, we show that the photosensory module of phyC exhibits a hypsochromically shifted Pr absorption maximum that is conserved across monocots and dicots. This spectral property is primarily determined by the GAF domain rather than by individual amino acid substitutions. Physiological analyses revealed that phyC contributes to the inhibition of hypocotyl elongation under red light conditions lacking shorter wavelength components, whereas its contribution is limited under white light conditions. These findings indicate that the hypsochromic shift in phyC provides a complementary mechanism for phytochrome signaling under specific light environments. Spectral overlap analysis further indicated that the hypsochromically shifted Pr absorption of phyC enhances photon capture under both direct sunlight and leaf-filtered light, although the magnitude of this effect is modest. Together, these findings indicate that the conserved hypsochromic shift in Pr absorption of phyC provides a complementary, context-dependent mechanism for phytochrome signaling, particularly under light environments in which phyB-mediated responses are less effective.

Indexed as

ArabidopsisArabidopsis ProteinsHypocotylPhytochromePhytochrome BLightRed LightSignal TransductionArabidopsis ProteinsPHYB protein, ArabidopsisPhytochromePhytochrome Bphytochrome C, ArabidopsisArabidopsis thalianaGAFhypocotyl elongationhypsochromic shiftphyBphyCphyFphytochromeSolanum lycopersicum

Identifiers

PMID42402218
PMCPMC13373367

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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.