Molecular mechanism of phototropin light signaling

Okajima, Koji

doi:10.1007/s10265-016-0783-6

Cited by 34Light effects on plantsPhotoreceptor and optogenetics researchPlant Molecular Biology Research

Molecular mechanism of phototropin light signaling

Okajima, Koji·2016·Journal of Plant Research

DOI 10.1007/s10265-016-0783-6

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Abstract

Phototropin (phot) is a blue light (BL) receptor kinase involved in the BL responses of several species, ranging from green algae to higher plants. Phot converts BL signals from the environment into biochemical signals that trigger cellular responses. In phot, the LOV1 and LOV2 domains of the N-terminal region utilize BL for cyclic photoreactions and regulate C-terminal serine/threonine kinase (STK) activity. LOV2-STK peptides are the smallest functional unit of phot and are useful for understanding regulation mechanisms. The combined analysis of spectroscopy and STK activity assay in Arabidopsis phots suggests that the decay speed of the photo-intermediate S390 in LOV2 is one of the factors contributing to light sensitive kinase activity. LOV2 and STK are thought to be adjacent to each other in LOV2-STK with small angle scattering (SAXS). BL irradiation induces LOV2-STK elongation, resulting in LOV2 shifting away from STK. The N- and C-terminal lateral regions of LOV2, A'α-helix, Jα-helix, and A'α/Aβ gap are responsible for the propagation of the BL signal to STK via conformational changes. The comparison between LOV2-STK and full-length phot from Chlamydomonas suggests that LOV1 is directly adjacent to LOV2 in LOV2-STK; therefore, LOV1 may indirectly regulate STK. The molecular mechanism of phot is discussed.

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LOV1 and LOV2 are structurally similar but not functionally identical; LOV1 regulates the light response of LOV2, which mainly controls phosphorylation of the kinase domain.
“Although LOV1 and LOV2 are structurally similar, they are not functionally identical. LOV1 regulates the light response of LOV2, which mainly controls phosphorylation of the kinase domain (Christie et al., 2015; Okajima, 2016).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Okajima, 2016
Phototropins are composed of approximately 1000 amino acids and two FMN domains, with an N-terminus containing two repeating conserved sequences LOV1 and LOV2, and a C-terminus STK domain that interconnects with LOV2.
“Phototropins are composed of approximately 1000 amino acids and two flavin mononucleotides (FMN) domain, and their N-terminus contains two repeating conserved sequences, LOV1 and LOV2. The C-terminus of phototropin is a serine/threonine kinase domain (STK) that interconnects with LOV2 (Christie, 2007; Okajima, 2016).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Okajima, 2016

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Authors: Okajima, K.
Affiliations: Keio University (JP)
Corresponding author: Okajima, Koji
ORCID: Okajima, Koji
Venue: Journal of Plant Research
Publisher: Springer Science and Business Media LLC
Published: 2016-01-27
Volume: 129
Issue: 2
Pages: 149-157
ISSN: 0918-9440 (ISSN-L)
1618-0860
DOI: 10.1007/s10265-016-0783-6
OpenAlex: W2264119264
Cited by: 34
References: 75
Citations by year: 2026: 4 · 2025: 4 · 2024: 1 · 2023: 2 · 2022: 2 · 2021: 5 · 2020: 3 · 2019: 4 · 2018: 2 · 2017: 4 · 2016: 3
FWCI: 5.05
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Journal of Plant Research (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
Keywords: phototropin, blue light signaling, LOV2 domain, conformational change
MeSH terms: Protein Domains, Chlamydomonas, DNA-Binding Proteins, Environment, Light, Models, Molecular, Phosphorylation, Protein Serine-Threonine Kinases, Arabidopsis, Protein Structure, Secondary, Arabidopsis Proteins, Light Signal Transduction, Phototropins

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Molecular mechanism of phototropin light signaling

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