Evidence map›Paper›PMID 25452667›Full record

ArticlePlant physiology2015

Iron-binding E3 ligase mediates iron response in plants by targeting basic helix-loop-helix transcription factors.

Devarshi Selote, Rozalynne Samira, Anna Matthiadis, Jeffrey W Gillikin, Terri A Long

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 136 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
136citing papers in PubMed, 1 pooled it
15.9field-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

136 citing papers in PubMed, 1 synthesis or guideline pooled it, 297 citations in OpenAlex.

  1. Pooled it
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76 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Devarshi SeloteDepartment of Plant and Microbial Biology, North Carolina State University, Raleigh, North Carolina 27695.
Rozalynne SamiraDepartment of Plant and Microbial Biology, North Carolina State University, Raleigh, North Carolina 27695.
Anna MatthiadisDepartment of Plant and Microbial Biology, North Carolina State University, Raleigh, North Carolina 27695.
Jeffrey W GillikinDepartment of Plant and Microbial Biology, North Carolina State University, Raleigh, North Carolina 27695.
Terri A LongDepartment of Plant and Microbial Biology, North Carolina State University, Raleigh, North Carolina 27695 talong@ncsu.edu.
North Carolina State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Iron uptake and metabolism are tightly regulated in both plants and animals. In Arabidopsis (Arabidopsis thaliana), BRUTUS (BTS), which contains three hemerythrin (HHE) domains and a Really Interesting New Gene (RING) domain, interacts with basic helix-loop-helix transcription factors that are capable of forming heterodimers with POPEYE (PYE), a positive regulator of the iron deficiency response. BTS has been shown to have E3 ligase capacity and to play a role in root growth, rhizosphere acidification, and iron reductase activity in response to iron deprivation. To further characterize the function of this protein, we examined the expression pattern of recombinant ProBTS::β-GLUCURONIDASE and found that it is expressed in developing embryos and other reproductive tissues, corresponding with its apparent role in reproductive growth and development. Our findings also indicate that the interactions between BTS and PYE-like (PYEL) basic helix-loop-helix transcription factors occur within the nucleus and are dependent on the presence of the RING domain. We provide evidence that BTS facilitates 26S proteasome-mediated degradation of PYEL proteins in the absence of iron. We also determined that, upon binding iron at the HHE domains, BTS is destabilized and that this destabilization relies on specific residues within the HHE domains. This study reveals an important and unique mechanism for plant iron homeostasis whereby an E3 ubiquitin ligase may posttranslationally control components of the transcriptional regulatory network involved in the iron deficiency response.

Indexed as

ArabidopsisArabidopsis ProteinsBasic Helix-Loop-Helix ProteinsIronIron-Binding ProteinsPlant RootsProteasome Endopeptidase ComplexUbiquitin-Protein LigasesArabidopsis ProteinsBasic Helix-Loop-Helix ProteinsIronIron-Binding ProteinsProteasome Endopeptidase ComplexUbiquitin-Protein Ligases

Identifiers

PMID25452667
PMCPMC4281009
OpenAlexW2019118425

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.