Evidence map›Paper›PMID 25944101›Full record

ArticleThe Plant cell2015

HEMERA Couples the Proteolysis and Transcriptional Activity of PHYTOCHROME INTERACTING FACTORs in Arabidopsis Photomorphogenesis.

Yongjian Qiu, Meina Li, Elise K Pasoreck, Lingyun Long, Yiting Shi, Rafaelo M Galvão, Conrad L Chou, He Wang, Amanda Y Sun, Yiyin C Zhang and 2 more

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
10.9field-weighted citation impact, top 2% 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

49 citing papers in PubMed, 78 citations in OpenAlex.

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  6. TheProceedings of the National Academy of Sciences of the United States of America · 2025
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  7. A circadian clock output functions independently of phyB to sustain daytime PIF3 degradation.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

12 authors at 1 institution in 1 country.

Yongjian QiuDepartment of Biology, Duke University, Durham, North Carolina 27708.
Meina LiDepartment of Biology, Duke University, Durham, North Carolina 27708.
Elise K PasoreckDepartment of Biology, Duke University, Durham, North Carolina 27708.
Lingyun LongDepartment of Biology, Duke University, Durham, North Carolina 27708.
Yiting ShiDepartment of Biology, Duke University, Durham, North Carolina 27708.
Rafaelo M GalvãoDepartment of Biology, Duke University, Durham, North Carolina 27708.
Conrad L ChouDepartment of Biology, Duke University, Durham, North Carolina 27708.
He WangDepartment of Biology, Duke University, Durham, North Carolina 27708.
Amanda Y SunDepartment of Biology, Duke University, Durham, North Carolina 27708.
Yiyin C ZhangDepartment of Biology, Duke University, Durham, North Carolina 27708.
Anna JiangDepartment of Biology, Duke University, Durham, North Carolina 27708.
Meng ChenDepartment of Biology, Duke University, Durham, North Carolina 27708 dr.mengchen@gmail.com.
Duke University · 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
NIGMS NIH HHS R01 GM087388NIGMS NIH HHS R01GM087388
6 · The paper itself

Abstract

Phytochromes (phys) are red and far-red photoreceptors that control plant development and growth by promoting the proteolysis of a family of antagonistically acting basic helix-loop-helix transcription factors, the PHYTOCHROME-INTERACTING FACTORs (PIFs). We have previously shown that the degradation of PIF1 and PIF3 requires HEMERA (HMR). However, the biochemical function of HMR and the mechanism by which it mediates PIF degradation remain unclear. Here, we provide genetic evidence that HMR acts upstream of PIFs in regulating hypocotyl growth. Surprisingly, genome-wide analysis of HMR- and PIF-dependent genes reveals that HMR is also required for the transactivation of a subset of PIF direct-target genes. We show that HMR interacts with all PIFs. The HMR-PIF interaction is mediated mainly by HMR's N-terminal half and PIFs' conserved active-phytochrome B binding motif. In addition, HMR possesses an acidic nine-amino-acid transcriptional activation domain (9aaTAD) and a loss-of-function mutation in this 9aaTAD impairs the expression of PIF target genes and the destruction of PIF1 and PIF3. Together, these in vivo results support a regulatory mechanism for PIFs in which HMR is a transcriptional coactivator binding directly to PIFs and the 9aaTAD of HMR couples the degradation of PIF1 and PIF3 with the transactivation of PIF target genes.

Indexed as

Transcriptional ActivationAmino Acid MotifsArabidopsisArabidopsis ProteinsBasic Helix-Loop-Helix ProteinsGene Expression ProfilingGene Expression Regulation, PlantHypocotylMicroarray AnalysisMutationPhytochromeProteolysisRecombinant Fusion ProteinsTranscription FactorsTwo-Hybrid System TechniquesArabidopsis ProteinsAt2g20180 protein, ArabidopsisBasic Helix-Loop-Helix ProteinsHMR protein, ArabidopsisPhytochromePIF3 protein, ArabidopsisRecombinant Fusion ProteinsTranscription Factors

Identifiers

PMID25944101
PMCPMC4456642
OpenAlexW1908991106

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.