Cited by 320Light effects on plantsPlant Molecular Biology ResearchPlant Parasitism and Resistance

Arabidopsis NPH3: A NPH1 Photoreceptor-Interacting Protein Essential for Phototropism

Motchoulski, Andrei, Liscum, Emmanuel·1999·Science

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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Crossref · 10.1126/science.286.5441.961

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38 of 38 references verified0 citation errors · 0 not checkable

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  • NPH3, RPT2, and PKS1 interact with PHOT1 and participate in the regulation of hypocotyl phototropism.

    “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).”
  • In the dark, NPH3 protein localizes to the cytoplasmic membrane and interacts with the N-terminus of the phot1 protein through its C-terminus.

    “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).”
  • Mutations in NPH3 cause Arabidopsis to 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.

    “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).”

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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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