Evidence map›Paper›PMID 22434039›Full record

ArticlePlant physiology2012

Serine/threonine/tyrosine protein kinase phosphorylates oleosin, a regulator of lipid metabolic functions.

Velayoudame Parthibane, Ramachandiran Iyappan, Anitha Vijayakumar, Varadarajan Venkateshwari, Ram Rajasekharan

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

29 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
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  4. Review
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  6. Article
  7. Molecular Machinery of Lipid Droplet Degradation and Turnover in Plants.International journal of molecular sciences · 2023
    Review
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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

5 authors at 3 institutions in 1 country.

Velayoudame ParthibaneDepartment of Biochemistry, Indian Institute of Science, Bangalore 560012, India.
Ramachandiran Iyappan
Anitha Vijayakumar
Varadarajan Venkateshwari
Ram Rajasekharan
Council of Scientific and Industrial Research · INCentral Institute of Medicinal and Aromatic Plants · INIndian Institute of Science Bangalore · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant oils are stored in oleosomes or oil bodies, which are surrounded by a monolayer of phospholipids embedded with oleosin proteins that stabilize the structure. Recently, a structural protein, Oleosin3 (OLE3), was shown to exhibit both monoacylglycerol acyltransferase and phospholipase A(2) activities. The regulation of these distinct dual activities in a single protein is unclear. Here, we report that a serine/threonine/tyrosine protein kinase phosphorylates oleosin. Using bimolecular fluorescence complementation analysis, we demonstrate that this kinase interacts with OLE3 and that the fluorescence was associated with chloroplasts. Oleosin-green fluorescent protein fusion protein was exclusively associated with the chloroplasts. Phosphorylated OLE3 exhibited reduced monoacylglycerol acyltransferase and increased phospholipase A(2) activities. Moreover, phosphatidylcholine and diacylglycerol activated oleosin phosphorylation, whereas lysophosphatidylcholine, oleic acid, and Ca(2+) inhibited phosphorylation. In addition, recombinant peanut (Arachis hypogaea) kinase was determined to predominantly phosphorylate serine residues, specifically serine-18 in OLE3. Phosphorylation levels of OLE3 during seed germination were determined to be higher than in developing peanut seeds. These findings provide direct evidence for the in vivo substrate selectivity of the dual-specificity kinase and demonstrate that the bifunctional activities of oleosin are regulated by phosphorylation.

Indexed as

Lipid MetabolismAcyltransferasesAmino Acid SequenceArachisCalciumChloroplastsCloning, MolecularDiglyceridesGenes, PlantGerminationGreen Fluorescent ProteinsMolecular Sequence DataOleic AcidPhosphatidylcholinesPhospholipases A2Phosphorylation2-acylglycerol O-acyltransferaseAcyltransferasesCalciumDiglyceridesGreen Fluorescent ProteinsOleic AcidPhosphatidylcholinesPhospholipases A2Plant ProteinsProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSerine

Identifiers

PMID22434039
PMCPMC3375988
OpenAlexW2056239986

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.