Evidence map›Paper›PMID 25096572›Full record

ArticleThe Journal of biological chemistry2014

Functional compartmentalization of the plasma membrane of neurons by a unique acyl chain composition of phospholipids.

Hideaki Kuge, Kana Akahori, Ken-Ichi Yagyu, Koichi Honke

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-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

19 citing papers in PubMed, 49 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

4 authors at 1 institution in 1 country.

Hideaki KugeDepartment of Biochemistry, Kochi University Medical School, Kohasu, Okocyou, Nankoku, Kochi 783-8505, Japan; Center for Innovate and Translational Medicine, and Kochi University Medical School, Kohasu, Okocyou, Nankoku, Kochi 783-8505, Japan. Electronic address: kugeh@kochi-u.ac.jp.
Kana AkahoriDepartment of Biochemistry, Kochi University Medical School, Kohasu, Okocyou, Nankoku, Kochi 783-8505, Japan.
Ken-Ichi YagyuScience Research Center, Kochi University Medical School, Kohasu, Okocyou, Nankoku, Kochi 783-8505, Japan.
Koichi HonkeDepartment of Biochemistry, Kochi University Medical School, Kohasu, Okocyou, Nankoku, Kochi 783-8505, Japan; Center for Innovate and Translational Medicine, and Kochi University Medical School, Kohasu, Okocyou, Nankoku, Kochi 783-8505, Japan. Electronic address: khonke@kochi-u.ac.jp.
Kōchi University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In neurons, the plasma membrane is functionally separated into several distinct segments. Neurons form these domains by delivering selected components to and by confining them within each segment of the membrane. Although some mechanisms of the delivery are elucidated, that of the confinement is unclear. We show here that 1-oleoyl-2-palmitoyl-phosphatidylcholine (OPPC), a unique molecular species of phospholipids, is concentrated at the protrusion tips of several neuronal culture cells and the presynaptic area of neuronal synapses of the mouse brain. In PC12 cells, NGF-stimulated neuronal differentiation induces a phospholipase A1 activity at the protrusion tips, which co-localizes with the OPPC domain. Inhibition of the phospholipase A1 activity leads to suppression of phospholipid remodeling in the tip membrane and results in disappearance of the OPPC at the tips. In these cells, confinement of dopamine transporter and Gαo proteins to the tip was also disrupted. These findings link the lateral distribution of the molecular species of phospholipids to the formation of functional segments in the plasma membrane of neurons and to the mechanism of protein confinement at the synapse.

Indexed as

AnimalsCell DifferentiationCell MembraneGTP-Binding Protein alpha SubunitsMiceNerve Growth FactorNeuronsPC12 CellsPhosphatidylcholinesPhospholipases A1RatsSynapses1-oleoyl-2-palmitoylphosphatidylcholineGTP-Binding Protein alpha SubunitsNerve Growth FactorPhosphatidylcholinesPhospholipases A1Cell PolarityMembrane CompartmentalizationNeurodifferentiationPhospholipase APhospholipid MetabolismPhospholipid RemodelingProtein TargetingSynapse

Identifiers

PMID25096572
PMCPMC4175321
OpenAlexW2039436414

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.