Evidence map›Paper›PMID 29199270›Full record

ArticleNature communications2017

Mechanism of early light signaling by the carboxy-terminal output module of Arabidopsis phytochrome B.

Yongjian Qiu, Elise K Pasoreck, Amit K Reddy, Akira Nagatani, Wenxiu Ma, Joanne Chory, Meng Chen

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
14.7field-weighted citation impact, top 1% 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

45 citing papers in PubMed, 83 citations in OpenAlex.

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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

7 authors at 4 institutions in 2 countries.

Yongjian QiuDepartment of Botany and Plant Sciences, Institute for Integrative Genome Biology, University of California, Riverside, CA, 92521, USA.
Elise K PasoreckDepartment of Biology, Duke University, Durham, NC, 27708, USA.
Amit K ReddyDepartment of Biology, Duke University, Durham, NC, 27708, USA.
Akira NagataniDepartment of Botany, Graduate School of Science, Kyoto University, Kyoto, 606-8502, Japan.
Wenxiu MaDepartment of Statistics, University of California, Riverside, CA, 92521, USA.
Joanne ChoryHoward Hughes Medical Institute, Plant Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, CA, 92037, USA.
Meng ChenDepartment of Botany and Plant Sciences, Institute for Integrative Genome Biology, University of California, Riverside, CA, 92521, USA. meng.chen@ucr.edu.ORCID http://orcid.org/0000-0003-0351-5897
University of California, Riverside · USDuke University · USKyoto University · JPSalk Institute for Biological Studies · US

Funding

Genetic Characterization of Phytochrome Nuclear Bodies in Plant Light SignalingR01GM087388 · NIGMS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI CHEN, MENG · 2010 to 2023
$5.8M
INITIAL EVENTS IN PHOTORECEPTOR SIGNALINGR01GM052413 · NIGMS · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI CHORY, JOANNE · 1995 to 2016
$5.4M
Acquisition of a Scalable Storage Cluster for Data Intensive NIH ResearchS10OD016290 · OD · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI GIRKE, THOMAS · 2014 to 2014
$593k
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM052413NIGMS NIH HHS R01 GM087388NIH HHS S10 OD016290
6 · The paper itself

Abstract

Plant phytochromes are thought to transduce light signals by mediating the degradation of phytochrome-interacting transcription factors (PIFs) through the N-terminal photosensory module, while the C-terminal module, including a histidine kinase-related domain (HKRD), does not participate in signaling. Here we show that the C-terminal module of Arabidopsis phytochrome B (PHYB) is sufficient to mediate the degradation of PIF3 specifically and to activate photosynthetic genes in the dark. The HKRD is a dimerization domain for PHYB homo and heterodimerization. A D1040V mutation, which disrupts the dimerization of HKRD and the interaction between C-terminal module and PIF3, abrogates PHYB nuclear accumulation, photobody biogenesis, and PIF3 degradation. By contrast, disrupting the interaction between PIF3 and PHYB's N-terminal module has little effect on PIF3 degradation. Together, this study demonstrates that the dimeric form of the C-terminal module plays important signaling roles by targeting PHYB to subnuclear photobodies and interacting with PIF3 to trigger its degradation.

Indexed as

LightLight Signal TransductionArabidopsisArabidopsis ProteinsBasic Helix-Loop-Helix ProteinsDimerizationMutationPhotosynthesisPhytochrome BProtein DomainsArabidopsis ProteinsBasic Helix-Loop-Helix ProteinsPHYB protein, ArabidopsisPhytochrome BPIF3 protein, Arabidopsis

Identifiers

PMID29199270
PMCPMC5712524
OpenAlexW2768388437

What OpenQuestion holds

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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.