Evidence map›Paper›PMID 41839911›Full record

ArticleNature communications2026

Oligomerization-competent PIF4 drives thermomorphogenesis through functional redundancy in transactivation and DNA binding.

Haibo Xiong, Abhishesh Bajracharya, Ranjeeta Odari, Eden E Bayer, Alyssa Stoner, Anupa Wasti, Jing Xi, Scott R Baerson, Meng Chen, Yongjian Qiu

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Haibo Xiong *Department of Biology, University of Mississippi, University, MS, USA.ORCID http://orcid.org/0000-0002-8787-9809
Abhishesh Bajracharya *Department of Biology, University of Mississippi, University, MS, USA.ORCID http://orcid.org/0000-0002-3114-2533
Ranjeeta OdariDepartment of Biology, University of Mississippi, University, MS, USA.ORCID http://orcid.org/0000-0002-8551-6799
Eden E BayerDepartment of Biology, University of Mississippi, University, MS, USA.ORCID http://orcid.org/0000-0003-3621-4097
Alyssa StonerDepartment of Biology, University of Mississippi, University, MS, USA.ORCID http://orcid.org/0009-0000-4228-306X
Anupa WastiDepartment of Biology, University of Mississippi, University, MS, USA.ORCID http://orcid.org/0009-0009-8485-6554
Jing XiNatural Products Utilization Research Unit, U.S. Department of Agriculture, Agricultural Research Service, University, MS, USA.ORCID http://orcid.org/0000-0003-0881-2356
Scott R BaersonNatural Products Utilization Research Unit, U.S. Department of Agriculture, Agricultural Research Service, University, MS, USA.
Meng ChenDepartment of Botany and Plant Sciences, Institute for Integrative Genome Biology, University of California, Riverside, CA, USA.ORCID http://orcid.org/0000-0003-0351-5897
Yongjian QiuDepartment of Biology, University of Mississippi, University, MS, USA. yqiu@olemiss.edu.ORCID http://orcid.org/0000-0002-1799-6305

Funding

Tracking Glycosylation State with Fluorinated Glycosides ProbesP20GM130460 · NIGMS · UNIVERSITY OF MISSISSIPPI · PI Joshua S Sharp · 2020 to 2026
$17.9M
Genetic Characterization of Phytochrome Nuclear Bodies in Plant Light SignalingR01GM087388 · NIGMS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI CHEN, MENG · 2010 to 2023
$5.8M
National Science Foundation (NSF) IOS-2200200National Science Foundation (NSF) IOS-2239963NIGMS NIH HHS P20 GM130460NIGMS NIH HHS R01 GM087388U.S. Department of Health & Human Services | National Institutes of Health (NIH) P20GM130460U.S. Department of Health & Human Services | National Institutes of Health (NIH) R01GM087388
6 · The paper itself

Abstract

Plants tailor their architecture to warm temperatures through the central transcription factor PHYTOCHROME-INTERACTING FACTOR 4 (PIF4). Here, we dissect how structured and disordered regions of PIF4 contribute to its function in thermomorphogenesis. A long N-terminal intrinsically disordered region (IDR) enables PIF4 to form low-mobility condensates. Within this IDR, we identify an acidic transactivation domain (TAD) and an extended basic segment that carries a nuclear-localization signal and the canonical basic motif of the basic helix-loop-helix (bHLH) domain. The basic segment is both necessary and sufficient to drive PIF4 condensate formation, while the TAD tunes condensate properties. Strikingly, alanine substitutions that abolish TAD-mediated transactivation, disrupt DNA binding, or greatly reduce phase-separation propensity have no significant effect on thermomorphogenetic hypocotyl elongation. By contrast, substituting twelve basic residues within the basic segment, which disrupts both DNA binding and HLH-mediated oligomerization, abolishes thermo-induced hypocotyl growth. These findings suggest that PIF4's oligomerization competence contributes significantly to thermomorphogenesis by enabling partner recruitment, allowing DNA-binding and transactivation functions to be supplied in trans.

Indexed as

ArabidopsisArabidopsis ProteinsBasic Helix-Loop-Helix ProteinsTranscriptional ActivationGene Expression Regulation, PlantHypocotylMorphogenesisProtein BindingProtein MultimerizationArabidopsis ProteinsBasic Helix-Loop-Helix ProteinsPIF4 protein, Arabidopsis

Identifiers

PMID41839911
PMCPMC13139478

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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.