Evidence map›Paper›PMID 20452984›Full record

ArticleThe Journal of biological chemistry2010

Temperature-sensitive post-translational regulation of plant omega-3 fatty-acid desaturases is mediated by the endoplasmic reticulum-associated degradation pathway.

Jami B O'Quin, Linda Bourassa, Daiyuan Zhang, Jay M Shockey, Satinder K Gidda, Spencer Fosnot, Kent D Chapman, Robert T Mullen, John M Dyer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

37 citing papers in PubMed, 88 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

9 authors at 5 institutions in 2 countries.

Jami B O'QuinDepartment of Biological Sciences, University of New Orleans, New Orleans, Louisiana 70124, USA.
Linda Bourassa
Daiyuan Zhang
Jay M Shockey
Satinder K Gidda
Spencer Fosnot
Kent D Chapman
Robert T Mullen
John M Dyer
Agricultural Research Service · USUnited States Department of Agriculture · USUniversity of Guelph · CAUniversity of New Orleans · USUniversity of North Texas · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Changes in ambient temperature represent a major physiological challenge to membranes of poikilothermic organisms. In plants, the endoplasmic reticulum (ER)-localized omega-3 fatty-acid desaturases (Fad3) increase the production of polyunsaturated fatty acids at cooler temperatures, but the FAD3 genes themselves are typically not up-regulated during this adaptive response. Here, we expressed two closely related plant FAD3 genes in yeast cells and found that their enzymes produced significantly different amounts of omega-3 fatty acids and that these differences correlated to differences in rates of protein turnover. Domain-swapping and mutagenesis experiments revealed that each protein contained a degradation signal in its N terminus and that the charge density of a PEST-like sequence within this region was largely responsible for the differences in rates of protein turnover. The half-life of each Fad3 protein was increased at cooler temperatures, and protein degradation required specific components of the ER-associated degradation pathway including the Cdc48 adaptor proteins Doa1, Shp1, and Ufd2. Expression of the Fad3 proteins in tobacco cells incubated with the proteasomal inhibitor MG132 further confirmed that they were degraded via the proteasomal pathway in plants. Collectively, these findings indicate that Fad3 protein abundance is regulated by a combination of cis-acting degradation signals and the ubiquitin-proteasome pathway and that modulation of Fad3 protein amounts in response to temperature may represent one mechanism of homeoviscous adaptation in plants.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceBrassicaCell MembraneEndoplasmic ReticulumFatty Acid DesaturasesLeupeptinsLipidsMolecular Sequence DataMutagenesisNicotianaOligonucleotide Array Sequence AnalysisProteasome Endopeptidase ComplexProteasome InhibitorsProteinsProtein Structure, Tertiarybenzyloxycarbonylleucyl-leucyl-leucine aldehydeFatty Acid DesaturasesLeupeptinsLipidsomega-3 fatty acid desaturaseProteasome Endopeptidase ComplexProteasome InhibitorsProteinsUbiquitin

Identifiers

PMID20452984
PMCPMC2898375
OpenAlexW1973804733

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.