Evidence map›Paper›PMID 38067638›Full record

ReviewMolecules (Basel, Switzerland)2023

Are There Lipid Membrane-Domain Subtypes in Neurons with Different Roles in Calcium Signaling?

Alejandro K Samhan-Arias, Joana Poejo, Dorinda Marques-da-Silva, Oscar H Martínez-Costa, Carlos Gutierrez-Merino

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

  1. Gangliosides in molecular interactions and cell regulation.The Journal of biological chemistry · 2026
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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 2 countries.

Alejandro K Samhan-AriasDepartamento de Bioquímica, Universidad Autónoma de Madrid (UAM), C/Arturo Duperier 4, 28029 Madrid, Spain.ORCID 0000-0001-9602-4848
Joana PoejoInstituto de Biomarcadores de Patologías Moleculares, Universidad de Extremadura, 06006 Badajoz, Spain.ORCID 0000-0001-8740-1074
Dorinda Marques-da-SilvaLSRE-Laboratory of Separation and Reaction Engineering and LCM-Laboratory of Catalysis and Materials, School of Management and Technology, Polytechnic Institute of Leiria, Morro do Lena-Alto do Vieiro, 2411-901 Leiria, Portugal.ORCID 0000-0003-0460-5421
Oscar H Martínez-CostaDepartamento de Bioquímica, Universidad Autónoma de Madrid (UAM), C/Arturo Duperier 4, 28029 Madrid, Spain.ORCID 0000-0003-4893-2205
Carlos Gutierrez-MerinoInstituto de Biomarcadores de Patologías Moleculares, Universidad de Extremadura, 06006 Badajoz, Spain.ORCID 0000-0003-3673-7007
Instituto de Investigaciones Biomédicas Sols-Morreale · ESUniversidad de Extremadura · ESInstituto Politécnico de Leiria · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipid membrane nanodomains or lipid rafts are 10-200 nm diameter size cholesterol- and sphingolipid-enriched domains of the plasma membrane, gathering many proteins with different roles. Isolation and characterization of plasma membrane proteins by differential centrifugation and proteomic studies have revealed a remarkable diversity of proteins in these domains. The limited size of the lipid membrane nanodomain challenges the simple possibility that all of them can coexist within the same lipid membrane domain. As caveolin-1, flotillin isoforms and gangliosides are currently used as neuronal lipid membrane nanodomain markers, we first analyzed the structural features of these components forming nanodomains at the plasma membrane since they are relevant for building supramolecular complexes constituted by these molecular signatures. Among the proteins associated with neuronal lipid membrane nanodomains, there are a large number of proteins that play major roles in calcium signaling, such as ionotropic and metabotropic receptors for neurotransmitters, calcium channels, and calcium pumps. This review highlights a large variation between the calcium signaling proteins that have been reported to be associated with isolated caveolin-1 and flotillin-lipid membrane nanodomains. Since these calcium signaling proteins are scattered in different locations of the neuronal plasma membrane, i.e., in presynapses, postsynapses, axonal or dendritic trees, or in the neuronal soma, our analysis suggests that different lipid membrane-domain subtypes should exist in neurons. Furthermore, we conclude that classification of lipid membrane domains by their content in calcium signaling proteins sheds light on the roles of these domains for neuronal activities that are dependent upon the intracellular calcium concentration. Some examples described in this review include the synaptic and metabolic activity, secretion of neurotransmitters and neuromodulators, neuronal excitability (long-term potentiation and long-term depression), axonal and dendritic growth but also neuronal cell survival and death.

Indexed as

Calcium SignalingCaveolin 1CalciumGangliosidesMembrane MicrodomainsNeuronsNeurotransmitter AgentsProteomicsCalciumCaveolin 1GangliosidesNeurotransmitter Agentsbraincalcium channelcaveolinflotillingangliosidelipid membrane domainslipid raftsmembrane domainsneuronNMDAP2XRPMCA

Identifiers

PMID38067638
PMCPMC10708093
OpenAlexW4389264812

What OpenQuestion holds

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LicenceCC BY
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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.