Evidence map›Paper›PMID 34675219›Full record

ArticleNature communications2021

Light-triggered and phosphorylation-dependent 14-3-3 association with NON-PHOTOTROPIC HYPOCOTYL 3 is required for hypocotyl phototropism.

Lea Reuter, Tanja Schmidt, Prabha Manishankar, Christian Throm, Jutta Keicher, Andrea Bock, Irina Droste-Borel, Claudia Oecking

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.8field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
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  13. Exploring lipid-protein interactions in plant membranes.Journal of experimental botany · 2024
    Review
  14. Article
  15. Article
  16. A 14-3-3 Protein-Encoding Gene,Plants (Basel, Switzerland) · 2023
    Article
  17. Article
  18. Article
  19. Review
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Lea Reuter *Center for Plant Molecular Biology (ZMBP), Plant Physiology, University of Tübingen, Tübingen, Germany.
Tanja Schmidt *Center for Plant Molecular Biology (ZMBP), Plant Physiology, University of Tübingen, Tübingen, Germany.ORCID 0000-0001-9203-8847
Prabha ManishankarCenter for Plant Molecular Biology (ZMBP), Plant Physiology, University of Tübingen, Tübingen, Germany.
Christian ThromCenter for Plant Molecular Biology (ZMBP), Plant Physiology, University of Tübingen, Tübingen, Germany.ORCID 0000-0003-2914-7025
Jutta KeicherCenter for Plant Molecular Biology (ZMBP), Plant Physiology, University of Tübingen, Tübingen, Germany.
Andrea BockCenter for Plant Molecular Biology (ZMBP), Plant Physiology, University of Tübingen, Tübingen, Germany.
Irina Droste-BorelProteome Center Tübingen, University of Tübingen, Tübingen, Germany.
Claudia OeckingCenter for Plant Molecular Biology (ZMBP), Plant Physiology, University of Tübingen, Tübingen, Germany. claudia.oecking@zmbp.uni-tuebingen.de.ORCID 0000-0003-0635-6457
University of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NON-PHOTOTROPIC HYPOCOTYL 3 (NPH3) is a key component of the auxin-dependent plant phototropic growth response. We report that NPH3 directly binds polyacidic phospholipids, required for plasma membrane association in darkness. We further demonstrate that blue light induces an immediate phosphorylation of a C-terminal 14-3-3 binding motif in NPH3. Subsequent association of 14-3-3 proteins is causal for the light-induced release of NPH3 from the membrane and accompanied by NPH3 dephosphorylation. In the cytosol, NPH3 dynamically transitions into membraneless condensate-like structures. The dephosphorylated state of the 14-3-3 binding site and NPH3 membrane recruitment are recoverable in darkness. NPH3 variants that constitutively localize either to the membrane or to condensates are non-functional, revealing a fundamental role of the 14-3-3 mediated dynamic change in NPH3 localization for auxin-dependent phototropism. This regulatory mechanism might be of general nature, given that several members of the NPH3-like family interact with 14-3-3 via a C-terminal motif.

Indexed as

14-3-3 ProteinsArabidopsisArabidopsis ProteinsCell MembraneHypocotylIndoleacetic AcidsLightPhosphorylationPhototropismProtein BindingProtein DomainsProtein Isoforms14-3-3 ProteinsArabidopsis ProteinsIndoleacetic AcidsNPH3 protein, ArabidopsisProtein Isoforms

Identifiers

PMID34675219
PMCPMC8531446
OpenAlexW3152831161

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.