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Arabidopsis NPH3: A NPH1 Photoreceptor-Interacting Protein Essential for Phototropism
Abstract
Phototropism of Arabidopsis thaliana seedlings in response to a blue light source is initiated by nonphototropic hypocotyl 1 (NPH1), a light-activated serine-threonine protein kinase. Mutations in three loci [ NPH2 , root phototropism 2 ( RPT2 ), and NPH3 ] disrupt early signaling occurring downstream of the NPH1 photoreceptor. The NPH3 gene, now cloned, encodes a NPH1-interacting protein. NPH3 is a member of a large protein family, apparently specific to higher plants, and may function as an adapter or scaffold protein to bring together the enzymatic components of a NPH1-activated phosphorelay.
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In the citing paper
“Interaction screening revealed that NPH3, RPT2, and PKS1 interact with PHOT1 and participate in the regulation of hypocotyl phototropism (Motchoulski and Liscum, 1999; Harper et al., 2000; Inada et al., 2004).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Motchoulski and Liscum, 1999
In the citing paper
“In the dark, NPH3 protein localizes to the cytoplasmic membrane and interacts with the N-terminus of the phot1 protein through its C-terminus (Motchoulski and Liscum, 1999).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Motchoulski and Liscum, 1999
In the citing paper
“Mutations in NPH3 causes Arabidopsis lose all-intensity blue light-induced phototropism, indicating that NPH3 regulates both PHOT1-mediated phototropism under low-fluence blue light and the PHOT1- and PHOT2-mediated high-fluence blue light response (Liscum and Briggs, 1996; Motchoulski and Liscum, 1999).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Motchoulski and Liscum, 1999
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Metadata
- Authors
- Motchoulski, A., & Liscum, E.
- Affiliations
- University of Missouri (US)
- Division of Biological Sciences, University of Missouri, Columbia, MO 65211, USA.
- Venue
- Science
- Published
- 1999-10-29
- Volume
- 286
- Issue
- 5441
- Pages
- 961-964
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2088376876
- Cited by
- 320
- References
- 37
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 17 · 2023: 7 · 2022: 9 · 2021: 17 · 2020: 12 · 2019: 5 · 2018: 7 · 2017: 13 · 2016: 9 · 2015: 12 · 2014: 15 · 2013: 12 · 2012: 18
- FWCI
- 15.45
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- 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 › Agricultural and Biological Sciences › Plant Science › Plant Parasitism and Resistance
- Keywords
- NPH3, phototropism, blue light photoreception, serine/threonine kinase, phosphorelay, scaffold proteins, Rpt2, Arabidopsis thaliana
- MeSH terms
- Amino Acid Sequence, Cell Membrane, Cloning, Molecular, Escherichia coli, Molecular Sequence Data, Phosphoproteins, Plant Proteins, Protein Binding, Protein Serine-Threonine Kinases, Arabidopsis, Photoreceptor Cells, Invertebrate, Phototropism, Two-Hybrid System Techniques, Arabidopsis Proteins
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