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Blue light‐induced association of phototropin 2 with the Golgi apparatus
Open accessAbstract
Summary: Phototropins 1 and 2 (phot1 and phot2) function as blue light (BL) photoreceptors for phototropism, chloroplast relocation, stomatal opening and leaf flattening in Arabidopsis thaliana . Phototropin consists of two functional domains, the N‐terminal photosensory domain and the C‐terminal Ser/Thr kinase domain. However, little is known about the signal transduction pathway that links the photoreceptors and the physiological responses downstream of BL perception. To understand the mechanisms by which phot2 initiates these responses, we transformed the phot1phot2 double mutant of Arabidopsis with constructs encoding translationally fused phot2:green fluorescent protein (P2G). P2G was fully functional for the phot2‐specific physiological responses in these transgenic plants. It localized strongly to the plasma membrane and weakly to the cytoplasm in the dark. Upon illumination with BL, punctate P2G staining was formed within a few minutes in addition to the constitutive plasma membrane staining. This punctate distribution pattern matched well with that of the Golgi‐localized KAM1ΔC:mRFP. Brefeldin A (BFA), an inhibitor of vesicle trafficking, induced accumulation of P2G around the perinuclear region even in darkness, but the punctate pattern was not observed. After treatment of these cells with BL, P2G exhibited the punctate distribution pattern that matched with that of the Golgi marker. Hence, the light‐dependent association of P2G with the Golgi apparatus was BFA‐insensitive. A structure/function analysis indicated that the kinase domain was essential for the Golgi localization of phot2. The BL‐induced Golgi localization of phot2 may be one of important signaling steps in the phot2 signal transduction pathway.
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“Under blue light irradiation, part of the PHOT1 protein detaches from the cell membrane and disperses in the cytoplasm, in contrast, some PHOT2 proteins can be coupled to the Golgi apparatus (Sakamoto and Briggs, 2002; Kong et al., 2006; Wan et al., 2008).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Kong et al., 2006
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“Although phot1 and phot2 do not possess a transmembrane domain, they localize to the inner side of the cytoplasmic membrane in the dark (Sakamoto and Briggs, 2002; Kong et al., 2006).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Kong et al., 2006
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Metadata
- Authors
- Kong, S., Suzuki, T., Tamura, K., Mochizuki, N., Hara‐Nishimura, I., & Nagatani, A.
- Affiliations
- Kyoto University (JP)
- Corresponding author
- Nagatani, Akira
- ORCID
- Venue
- The Plant Journal
- Publisher
- Wiley
- Published
- 2006-02-17
- Volume
- 45
- Issue
- 6
- Pages
- 994-1005
- ISSN
- 0960-7412 (ISSN-L)
- 1365-313X
- OpenAlex
- W2049111667
- Cited by
- 152
- References
- 50
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 6 · 2023: 1 · 2022: 7 · 2021: 7 · 2020: 8 · 2019: 4 · 2018: 7 · 2017: 1 · 2016: 10 · 2015: 9 · 2014: 14 · 2013: 10 · 2012: 14
- FWCI
- 12.31
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Plant Journal (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (13440239)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Keywords
- phototropin 2, blue-light photoreceptor, Golgi apparatus, Golgi localization, phototropism, signal transduction, kinase domain, plasma membrane, vesicle trafficking, Arabidopsis thaliana, stomatal opening
- MeSH terms
- Cell Membrane, Cytoplasm, Golgi Apparatus, Light, Phosphoproteins, Recombinant Fusion Proteins, Immunoblotting, Signal Transduction, Protein Serine-Threonine Kinases, Arabidopsis, Protein Structure, Tertiary, Arabidopsis Proteins, Plants, Genetically Modified
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