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Modulation of Phototropic Responsiveness in Arabidopsis through Ubiquitination of Phototropin 1 by the CUL3-Ring E3 Ubiquitin Ligase CRL3NPH3
Open accessAbstract
Plant phototropism is an adaptive response to changes in light direction, quantity, and quality that results in optimization of photosynthetic light harvesting, as well as water and nutrient acquisition. Though several components of the phototropic signal response pathway have been identified in recent years, including the blue light (BL) receptors phototropin1 (phot1) and phot2, much remains unknown. Here, we show that the phot1-interacting protein NONPHOTOTROPIC HYPOCOTYL3 (NPH3) functions as a substrate adapter in a CULLIN3-based E3 ubiquitin ligase, CRL3NPH3. Under low-intensity BL, CRL3NPH3 mediates the mono/multiubiquitination of phot1, likely marking it for clathrin-dependent internalization from the plasma membrane. In high-intensity BL, phot1 is both mono/multi- and polyubiquitinated by CRL3NPH3, with the latter event targeting phot1 for 26S proteasome-mediated degradation. Polyubiquitination and subsequent degradation of phot1 under high-intensity BL likely represent means of receptor desensitization, while mono/multiubiquitination-stimulated internalization of phot1 may be coupled to BL-induced relocalization of hormone (auxin) transporters.
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“CUL3 is required for blue light-induced ubiquitination of PHOT1, and PHOT1 ubiquitination is thought to be involved in phototropism (Salomon et al., 1997; Thomann et al., 2005; Roberts et al., 2011).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Roberts et al., 2011
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Metadata
- Authors
- Roberts, D., Pedmale, U. V., Morrow, J., Sachdev, S., Lechner, E., Tang, X., Zheng, N., Hannink, M., Genschik, P., & Liscum, E.
- Affiliations
- University of Missouri (US)
- Centre National de la Recherche Scientifique (FR)
- Howard Hughes Medical Institute (US)
- Division of Biological Sciences, University of Missouri, Columbia, Missouri 65211
- ORCID
- Venue
- The Plant Cell
- Publisher
- Oxford University Press (OUP)
- Published
- 2011-10-01
- Volume
- 23
- Issue
- 10
- Pages
- 3627-3640
- ISSN
- 1040-4651 (ISSN-L)
- 1532-298X
- PMC
- PMC3229139
- OpenAlex
- W2171122839
- Cited by
- 150
- References
- 70
- Citations by year
- 2026: 7 · 2025: 9 · 2024: 12 · 2023: 7 · 2022: 9 · 2021: 12 · 2020: 8 · 2019: 4 · 2018: 10 · 2017: 10 · 2016: 8 · 2015: 9 · 2014: 18 · 2013: 11 · 2012: 16
- FWCI
- 17.36
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model (vor)
- Locations
- The Plant Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Cold Spring Harbor Laboratory Institutional Repository (Cold Spring Harbor Laboratory) (acceptedVersion)
- HAL (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- University of Missouri
- National Cancer Institute (R01CA107134)
- National Institute of General Medical Sciences (T34-GM008396, T32GM008396)
- National Center for Complementary and Integrative Health (1R01-AT003389)
- 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 › Ubiquitin and proteasome pathways
- Keywords
- phototropism, phototropin 1, NPH3, ubiquitination, polyubiquitination, monoubiquitination, 26S proteasome degradation, auxin transporters, blue light signaling, Arabidopsis thaliana
- MeSH terms
- Animals, Biological Transport, Carrier Proteins, Cell Line, Chlorocebus aethiops, Indoleacetic Acids, Lepidoptera, Light, Mutation, Phosphoproteins, Nicotiana, Protein Serine-Threonine Kinases, Arabidopsis, Plant Leaves, Phototropism, Arabidopsis Proteins, Seedlings, Ubiquitin-Protein Ligases, Cullin Proteins, Proteasome Endopeptidase Complex, Ubiquitination, Light Signal Transduction, Phototropins, Proteolysis
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