Evidence map›Paper›PMID 40638049›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2025

Identification of Cytosol-Facing Organelle Membrane-Proximal Proteins via Proximity-Dependent Biotinylation.

Xinyue Bao, Xiaoyan Zhang, Huifang Jia, Xiaohong Zhu

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Article in Methods in molecular biology (Clifton, N.J.), 2025. 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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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

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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

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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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.

Xinyue BaoState Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, Kaifeng, China.
Xiaoyan ZhangState Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, Kaifeng, China.
Huifang JiaState Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, Kaifeng, China.
Xiaohong ZhuState Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, Kaifeng, China. zhuxiaohong@henu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Organelle membrane (OM)-resident or -proximal proteins that face the cytosol play a critical role in the import and exchange of ions, metabolites, and proteins between subcellular compartments, thereby regulating organelle biogenesis and function. However, the identification and functional characterization of these proteins pose challenges due to their dynamic spatial and temporal nature. We introduce a proximity labeling system using biotin ligase-mediated protein biotinylation in live Arabidopsis thaliana cells. This chapter outlines a detailed step-by-step protocol for identifying cytosol-facing OM-resident or -proximal proteins of mitochondria, chloroplasts, and peroxisomes in plant cells. This protocol can be adapted to identify cytosol-facing OM-resident and/or proximal proteins of any subcellular compartments of interest, as well as to map their spatiotemporal profiles under various stress conditions. The protocol described includes the following key steps: (1) sample preparation; (2) optimization of biotin labeling conditions; (3) enrichment of biotinylated proteins for liquid chromatography-tandem mass spectrometry (LC-MS/MS); (4) validation of identified candidate proteins.

Indexed as

ArabidopsisArabidopsis ProteinsBiotinylationCytosolIntracellular MembranesMembrane ProteinsBiotinChloroplastsChromatography, LiquidMitochondriaPeroxisomesTandem Mass SpectrometryArabidopsis ProteinsBiotinMembrane ProteinsArabidopsis thalianaBiotin protein ligaseOrganellar quality controlOrganelle membrane proximal proteinOrganelle membrane proximity labelingProximity labeling

Identifiers

PMID40638049

What OpenQuestion holds

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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.