Regulation of Phototropic Signaling in Arabidopsis via Phosphorylation State Changes in the Phototropin 1-interacting Protein NPH3

Pedmale, Ullas V.; Liscum, Emmanuel

doi:10.1074/jbc.m702551200

Cited by 169Light effects on plantsPlant Molecular Biology ResearchPlant Parasitism and Resistance

Regulation of Phototropic Signaling in Arabidopsis via Phosphorylation State Changes in the Phototropin 1-interacting Protein NPH3

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Pedmale, Ullas V., Liscum, Emmanuel·2007·Journal of Biological Chemistry

DOI 10.1074/jbc.m702551200

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Abstract

Phototropism, or the directional growth (curvature) of various organs toward or away from incident light, represents a ubiquitous adaptive response within the plant kingdom. This response is initiated through the sensing of directional blue light (BL) by a small family of photoreceptors known as the phototropins. Of the two phototropins present in the model plant Arabidopsis thaliana, phot1 (phototropin 1) is the dominant receptor controlling phototropism. Absorption of BL by the sensory portion of phot1 leads, as in other plant phototropins, to activation of a C-terminal serine/threonine protein kinase domain, which is tightly coupled with phototropic responsiveness. Of the five phot1-interacting proteins identified to date, only one, NPH3 (non-phototropic hypocotyl 3), is essential for all phot1-dependent phototropic responses, yet little is known about how phot1 signals through NPH3. Here, we show that, in dark-grown seedlings, NPH3 exists as a phosphorylated protein and that BL stimulates its dephosphorylation. phot1 is necessary for this response and appears to regulate the activity of a type 1 protein phosphatase that catalyzes the reaction. The abrogation of both BL-dependent dephosphorylation of NPH3 and development of phototropic curvatures by protein phosphatase inhibitors further suggests that this post-translational modification represents a crucial event in phot1-dependent phototropism. Given that NPH3 may represent a core component of a CUL3-based ubiquitin-protein ligase (E3), we hypothesize that the phosphorylation state of NPH3 determines the functional status of such an E3 and that differential regulation of this E3 is required for normal phototropic responsiveness.

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Under blue light, NPH3 undergoes PHOT1-dependent dephosphorylation, detaches from the plasma membrane, and enters the cytoplasm to form aggregates.
“Under blue light, NPH3 undergoes PHOT1-dependent dephosphorylation, detaches from the plasma membrane, and enters the cytoplasm to form aggregates (Pedmale and Liscum, 2007; Sullivan et al., 2019).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Pedmale and Liscum, 2007

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“Under blue light, NPH3 undergoes PHOT1-dependent dephosphorylation, detaches from the plasma membrane, and enters the cytoplasm to form aggregates (Pedmale and Liscum, 2007; Sullivan et al., 2019).”
Background

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Authors: Pedmale, U. V., & Liscum, E.
Affiliations: University of Missouri (US)
ORCID: Pedmale, Ullas V.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2007-07
Volume: 282
Issue: 27
Pages: 19992-20001
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m702551200
OpenAlex: W2089361074
Cited by: 169
References: 93
Citations by year: 2026: 4 · 2025: 6 · 2024: 7 · 2023: 17 · 2022: 4 · 2021: 11 · 2020: 6 · 2019: 10 · 2018: 10 · 2017: 7 · 2016: 7 · 2015: 9 · 2014: 8 · 2013: 7 · 2012: 13
FWCI: 14.18
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-nd
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 4872 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by-nc-nd)
PubMed (publishedVersion)
Cold Spring Harbor Laboratory Institutional Repository (Cold Spring Harbor Laboratory) (acceptedVersion)
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: phototropism, phototropin 1, NPH3, blue light signaling, protein phosphorylation, dephosphorylation, protein phosphatase, E3 ubiquitin ligase, Arabidopsis thaliana, post-translational modification
MeSH terms: Carrier Proteins, Enzyme Inhibitors, Flavoproteins, Phosphoprotein Phosphatases, Protein Processing, Post-Translational, Signal Transduction, Arabidopsis, Phototropism, Arabidopsis Proteins, Seedlings, Ubiquitin-Protein Ligases, Cryptochromes

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Regulation of Phototropic Signaling in Arabidopsis via Phosphorylation State Changes in the Phototropin 1-interacting Protein NPH3

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