Actin-dependent plastid movement is required for motive force generation in directional nuclear movement in plants
Open accessAbstract
Significance: High-light–induced avoidance movements of chloroplasts and nuclei from the leaf cell surface to the side walls are essential for minimizing damage from strong visible light and UV light, respectively. Phototropins, blue-light photoreceptors, regulate short actin filaments on the plasma membrane side of chloroplasts, allowing chloroplasts to move autonomously in response to light. We show that some plastids attach to the nucleus, and that their actin-dependent movements are essential for light-induced nuclear movement in the Arabidopsis leaf cell. Indeed, nuclei without plastid attachments did not exhibit blue-light-induced movement. Our results demonstrate that nuclei are incapable of autonomously moving in response to light, and that the close association between nuclei and plastids is essential for their cooperative movements and functions.
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The CHUP1 protein is key for removing chloroplasts from the plasma membrane and depositing them at the bottom of the cell without moving under any light conditions.
“Analysis of the chup1 mutant in Arabidopsis revealed the key role of the CHUP1 protein in removing chloroplasts from the plasma membrane and depositing them at the bottom of the cell without moving under any light conditions”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Higa et al., 2014
In “Mutant Plants Deficient in Chloroplast Photorelocation Movement” (page unavailable), the paper says chloroplasts in chup1 cells were dissociated from the plasma membrane and moved rapidly—not that CHUP1 removes them or leaves them motionless. The cell-bottom observation concerns nuclei in darkness; the cited passages do not describe CHUP1 depositing chloroplasts there under all light conditions. (LLM, conf=0.89)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredThe hydrophobic section of CHUP1 binds to the chloroplast outer membrane and can connect the chloroplast to the coiled-coil region of the plasma membrane, F-actin binding site, and C-terminal conserved region.
“The hydrophobic section of CHUP1 protein binds to the chloroplast outer membrane, which can connect the chloroplast to the coiled-coil region of the plasma membrane, F-actin binding site, and C-terminal conserved region”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Higa et al., 2014
The section on mutants deficient in chloroplast photorelocation movement describes CHUP1 as an actin-binding protein localized on chloroplasts and plastids. The paper’s references also identify CHUP1 as a chloroplast outer-envelope protein involved in anchorage to the plasma membrane. Our copy does not describe a hydrophobic section binding the outer membrane or the claimed connections to coiled-coil, F-actin-binding, and C-terminal conserved regions (pages unavailable). (LLM, conf=0.84)
Experimental — accuracy not yet measured
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Cites
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Suetsugu, N., Higa, T., Kong, S.-G., & Wada, M. (2015) · Plant Physiology · doi:10.1104/pp.15.00214 · Cited by 51 · see citing works
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Self-citationThe action of enhancing weak light capture via phototropic growth and chloroplast movement in plants
Xin, G.-Y., Li, L.-P., Wang, P.-T., Li, X.-Y., Han, Y.-J., & Zhao, X. (2022) · Stress Biology · doi:10.1007/s44154-022-00066-x · Cited by 17 · see citing works
“The hydrophobic section of CHUP1 protein binds to the chloroplast outer membrane, which can connect the chloroplast to the coiled-coil region of the plasma membrane, F-actin binding site, and C-terminal conserved region (Oikawa et al., 2008; Higa et al., 2014).”
BackgroundGustav Senn (1875–1945): The pioneer of chloroplast movement research
Kataoka, H. (2015) · Journal of Integrative Plant Biology · doi:10.1111/jipb.12311 · Cited by 12 · see citing works
- Authors
- Higa, T., Suetsugu, N., Kong, S.-G., & Wada, M.
- Affiliations
- Kyushu University (JP)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2014-03-03
- Volume
- 111
- Issue
- 11
- Pages
- 4327-4331
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3964046
- OpenAlex
- W2142389989
- Cited by
- 70
- References
- 22
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 4 · 2023: 5 · 2022: 9 · 2021: 6 · 2020: 6 · 2019: 3 · 2018: 8 · 2017: 5 · 2016: 9 · 2015: 8 · 2014: 2
- FWCI
- 9.35
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education, Science and Technology
- Japan Society for the Promotion of Science (25440140, 25120721, 25251033)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- nuclear movement, F-actin, nuclear positioning, phototropin, blue light signaling, cytoskeleton, Arabidopsis thaliana, leaf epidermal cells
- MeSH terms
- Actins, Biomechanical Phenomena, Cell Nucleus, Light, Microscopy, Fluorescence, Movement, Arabidopsis, Plastids, Plant Leaves, Microscopy, Confocal, Time-Lapse Imaging
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