THRUMIN1 Is a Light-Regulated Actin-Bundling Protein Involved in Chloroplast Motility
Open accessAbstract
Chloroplast movement in response to changing light conditions optimizes photosynthetic light absorption. This repositioning is stimulated by blue light perceived via the phototropin photoreceptors and is transduced to the actin cytoskeleton. Some actin-based motility systems use filament reorganizations rather than myosin-based translocations. Recent research favors the hypothesis that chloroplast movement is driven by actin reorganization at the plasma membrane, but no proteins affecting chloroplast movements have been shown to associate with both the plasma membrane and actin filaments in vivo. Here we identified THRUMIN1 as a critical link between phototropin photoreceptor activity at the plasma membrane and actin-dependent chloroplast movements. THRUMIN1 bundles filamentous actin in vitro, and it localizes to the plasma membrane and displays light- and phototropin-dependent localization to microfilaments in vivo. These results suggest that phototropin-induced actin bundling via THRUMIN1 is important for chloroplast movement. A mammalian homolog of THRUMIN1, GRXCR1, has been implicated in auditory responses and hair cell stereocilla development as a regulator of actin architecture. Studies of THRUMIN1 will help elucidate the function of this family of eukaryotic proteins.
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Through its myristoylated N-terminus, THRUMIN1 localizes to the plasma membrane and alters actin filaments in a blue light- and phototropin-dependent manner.
“Through its myristoylated N-terminus, THRUMIN1 localizes to the plasma membrane and alters actin filaments in a blue light- and phototropin-dependent manner”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Whippo et al., 2011
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Cytoskeletal control of development and environmental adaptation in plants
Zhang, Y., Li, J., Xiang, Y., Wang, P., Le, J., Jing, Y., Wang, T., Wang, X., Zhu, L., Qian, D., et al. (2025) · Science China Life Sciences · doi:10.1007/s11427-024-3067-y
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- Authors
- Whippo, C. W., Khurana, P., Davis, P. A., DeBlasio, S. L., DeSloover, D., Staiger, C. J., & Hangarter, R. P.
- Affiliations
- Indiana University Bloomington (US)
- Purdue University West Lafayette (US)
- Corresponding author
- Hangarter, Roger P.
- ORCID
- Venue
- Current Biology
- Publisher
- Elsevier BV
- Published
- 2011-01
- Volume
- 21
- Issue
- 1
- Pages
- 59-64
- ISSN
- 0960-9822 (ISSN-L)
- OpenAlex
- W1981523943
- Cited by
- 83
- References
- 23
- Citations by year
- 2025: 6 · 2024: 5 · 2023: 5 · 2022: 3 · 2021: 3 · 2020: 5 · 2019: 2 · 2018: 4 · 2017: 4 · 2016: 8 · 2015: 3 · 2014: 8 · 2013: 5 · 2012: 10
- FWCI
- 10.36
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Current Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- U.S. Department of Energy
- Indiana University Bloomington
- Basic Energy Sciences
- 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 › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- actin bundling, phototropin, blue light signaling, actin cytoskeleton, plasma membrane, actin reorganization
- MeSH terms
- Actins, Chloroplasts, Cytoskeleton, Light, Microfilament Proteins, Arabidopsis, Gene Expression Regulation, Plant, Plant Leaves, Arabidopsis Proteins
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