Evidence map›Paper›PMID 42613524›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Elucidation of Ganglioside Microdomains Using Proximity Labeling.

Norihiro Kotani, Arisa Miyagawa-Yamaguchi, Koichi Honke

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Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Norihiro KotaniDepartment of Pharmacology, Saitama Medical University, Iruma-gun, Saitama, Japan. kotani@saitama-med.ac.jp.
Arisa Miyagawa-YamaguchiDepartment of Biochemistry, Kochi University Medical School, Nankoku, Kochi, Japan.
Koichi HonkeDepartment of Biochemistry, Kochi University Medical School, Nankoku, Kochi, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It has long been known that lipid microdomain structures (also called "lipid rafts") are formed in the cell membrane, and gangliosides are concentrated in these domains. Many functional molecules (membrane proteins, receptors, and their associated signaling molecules, etc.) are concentrated in these domains along with gangliosides, and it has been pointed out that these domains play an important role in signal transduction, for instance, from outside the cell. Interestingly, it has been pointed out that each microdomain contains different types of gangliosides and functional molecules, and it is highly likely that the functions of the microdomain structures are different from each other. However, it has been difficult to specifically analyze individual microdomains, for instance, such as the microdomain composed of GM1, whereas the methods for analyzing all microdomains existed in same cell have been established. Here, we explain a method for analyzing "individual" microdomains by each ganglioside using a proximity labeling technique.

Indexed as

GangliosidesMembrane MicrodomainsStaining and LabelingAnimalsHumansGangliosidesArylazideEnzyme-mediated activation of radical sourcesHorseradish peroxidaseLipid–protein interactionsLipid raftPlasma membraneProximity labelingProximity proteomicsTyramide

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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.