Evidence map›Paper›PMID 23673981›Full record

ArticleThe Plant cell2013

Loss of plastoglobule kinases ABC1K1 and ABC1K3 causes conditional degreening, modified prenyl-lipids, and recruitment of the jasmonic acid pathway.

Peter K Lundquist, Anton Poliakov, Lisa Giacomelli, Giulia Friso, Mason Appel, Ryan P McQuinn, Stuart B Krasnoff, Elden Rowland, Lalit Ponnala, Qi Sun and 1 more

Open access · greenAbstract 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 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

50 citing papers in PubMed, 112 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

11 authors at 3 institutions in 1 country.

Peter K LundquistDepartment of Plant Biology, Cornell University, Ithaca, New York 14853, USA.
Anton Poliakov
Lisa Giacomelli
Giulia Friso
Mason Appel
Ryan P McQuinn
Stuart B Krasnoff
Elden Rowland
Lalit Ponnala
Qi Sun
Klaas J van Wijk
Cornell University · USIthaca College · USRobert W. Holley Center for Agriculture & Health · US

Funding

CHEMISTRY OF BIOLOGICAL SYSTEMST32GM008500 · NIGMS · CORNELL UNIVERSITY ITHACA · PI LIN, HENING · 1996 to 2020
$5.4M
NIGMS NIH HHS 5T32GM008500NIGMS NIH HHS T32 GM008500
6 · The paper itself

Abstract

Plastoglobules (PGs) are plastid lipid-protein particles. This study examines the function of PG-localized kinases ABC1K1 and ABC1K3 in Arabidopsis thaliana. Several lines of evidence suggested that ABC1K1 and ABC1K3 form a protein complex. Null mutants for both genes (abc1k1 and abc1k3) and the double mutant (k1 k3) displayed rapid chlorosis upon high light stress. Also, k1 k3 showed a slower, but irreversible, senescence-like phenotype during moderate light stress that was phenocopied by drought and nitrogen limitation, but not cold stress. This senescence-like phenotype involved degradation of the photosystem II core and upregulation of chlorophyll degradation. The senescence-like phenotype was independent of the EXECUTER pathway that mediates genetically controlled cell death from the chloroplast and correlated with increased levels of the singlet oxygen-derived carotenoid β-cyclocitral, a retrograde plastid signal. Total PG volume increased during light stress in wild type and k1 k3 plants, but with different size distributions. Isolated PGs from k1 k3 showed a modified prenyl-lipid composition, suggesting reduced activity of PG-localized tocopherol cyclase (VTE1), and was consistent with loss of carotenoid cleavage dioxygenase 4. Plastid jasmonate biosynthesis enzymes were recruited to the k1 k3 PGs but not wild-type PGs, while pheophytinase, which is involved in chlorophyll degradation, was induced in k1 k3 and not wild-type plants and was localized to PGs. Thus, the ABC1K1/3 complex contributes to PG function in prenyl-lipid metabolism, stress response, and thylakoid remodeling.

Indexed as

ArabidopsisArabidopsis ProteinsBiosynthetic PathwaysChloroplastsCyclopentanesElectrophoresis, Polyacrylamide GelGene Expression Regulation, EnzymologicGene Expression Regulation, PlantImmunoblottingLightMass SpectrometryMicroscopy, ElectronMultiprotein ComplexesMutationOxidative StressOxylipinsABC1K1 protein, ArabidopsisArabidopsis ProteinsCyclopentanesjasmonic acidMultiprotein ComplexesOxylipinsProtein KinasesProtein Serine-Threonine Kinases

Identifiers

PMID23673981
PMCPMC3694708
OpenAlexW2140483816

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.