Evidence map›Paper›PMID 23404890›Full record

ArticleThe Plant cell2013

The SUD1 gene encodes a putative E3 ubiquitin ligase and is a positive regulator of 3-hydroxy-3-methylglutaryl coenzyme a reductase activity in Arabidopsis.

Verónica G Doblas, Vítor Amorim-Silva, David Posé, Abel Rosado, Alicia Esteban, Montserrat Arró, Herlander Azevedo, Aureliano Bombarely, Omar Borsani, Victoriano Valpuesta and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
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  6. Review
  7. Article
  8. Mechanisms of Endoplasmic Reticulum Protein Homeostasis in Plants.International journal of molecular sciences · 2023
    Review
  9. Article
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  18. Article
  19. Disruption of the NFrontiers in plant science · 2021
    Article
  20. Article
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

13 authors at 5 institutions in 3 countries.

Verónica G DoblasInstituto de Hortofruticultura Subtropical y Mediterránea, Universidad de Málaga-Consejo Superior de Investigaciones Científicas, Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Universidad de Málaga, 29071 Malaga, Spain.
Vítor Amorim-Silva
David Posé
Abel Rosado
Alicia Esteban
Montserrat Arró
Herlander Azevedo
Aureliano Bombarely
Omar Borsani
Victoriano Valpuesta
Albert Ferrer
Rui M Tavares
Miguel A Botella
Consejo Superior de Investigaciones Científicas · ESUniversidad de Málaga · ESUniversity of Minho · PTUniversidad de la República · UYUniversitat Autònoma de Barcelona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) enzyme catalyzes the major rate-limiting step of the mevalonic acid (MVA) pathway from which sterols and other isoprenoids are synthesized. In contrast with our extensive knowledge of the regulation of HMGR in yeast and animals, little is known about this process in plants. To identify regulatory components of the MVA pathway in plants, we performed a genetic screen for second-site suppressor mutations of the Arabidopsis thaliana highly drought-sensitive drought hypersensitive2 (dry2) mutant that shows decreased squalene epoxidase activity. We show that mutations in SUPPRESSOR OF DRY2 DEFECTS1 (SUD1) gene recover most developmental defects in dry2 through changes in HMGR activity. SUD1 encodes a putative E3 ubiquitin ligase that shows sequence and structural similarity to yeast Degradation of α factor (Doα10) and human TEB4, components of the endoplasmic reticulum-associated degradation C (ERAD-C) pathway. While in yeast and animals, the alternative ERAD-L/ERAD-M pathway regulates HMGR activity by controlling protein stability, SUD1 regulates HMGR activity without apparent changes in protein content. These results highlight similarities, as well as important mechanistic differences, among the components involved in HMGR regulation in plants, yeast, and animals.

Indexed as

ArabidopsisArabidopsis ProteinsHumansHydroxymethylglutaryl CoA ReductasesMembrane ProteinsMevalonic AcidMutationPhenotypePlant RootsPlants, Genetically ModifiedPlant ShootsSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSterolsUbiquitin-Protein LigasesArabidopsis ProteinsCER9 protein, ArabidopsisHydroxymethylglutaryl CoA ReductasesMARCHF6 protein, humanMembrane ProteinsMevalonic AcidSaccharomyces cerevisiae ProteinsSSM4 protein, S cerevisiaeSterolsUbiquitin-Protein Ligases

Identifiers

PMID23404890
PMCPMC3608789
OpenAlexW2101783385

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.