Advanced imaging techniques for studying protein phase separation in living cells and at single-molecule level.

Assembly dynamics Biomolecular condensate Fluidity LLPS Nucleation Single molecule approaches Spatiotemporal resolution

Journal

Current opinion in chemical biology
ISSN: 1879-0402
Titre abrégé: Curr Opin Chem Biol
Pays: England
ID NLM: 9811312

Informations de publication

Date de publication:
10 2023
Historique:
received: 31 03 2023
revised: 04 06 2023
accepted: 24 06 2023
pmc-release: 01 10 2024
medline: 22 9 2023
pubmed: 1 8 2023
entrez: 31 7 2023
Statut: ppublish

Résumé

Protein-protein and protein-RNA interactions are essential for cell function and survival. These interactions facilitate the formation of ribonucleoprotein complexes and biomolecular condensates via phase separation. Such assembly is involved in transcription, splicing, translation and stress response. When dysregulated, proteins and RNA can undergo irreversible aggregation which can be cytotoxic and pathogenic. Despite technical advances in investigating biomolecular condensates, achieving the necessary spatiotemporal resolution to deduce the parameters that govern their assembly and behavior has been challenging. Many laboratories have applied advanced microscopy methods for imaging condensates. For example, single molecule imaging methods have enabled the detection of RNA-protein interaction, protein-protein interaction, protein conformational dynamics, and diffusional motion of molecules that report on the intrinsic molecular interactions underlying liquid-liquid phase separation. This review will outline advances in both microscopy and spectroscopy techniques which allow single molecule detection and imaging, and how these techniques can be used to probe unique aspects of biomolecular condensates.

Identifiants

pubmed: 37523989
pii: S1367-5931(23)00109-6
doi: 10.1016/j.cbpa.2023.102371
pmc: PMC10528199
mid: NIHMS1915133
pii:
doi:

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

102371

Subventions

Organisme : NIA NIH HHS
ID : RF1 AG071326
Pays : United States
Organisme : NINDS NIH HHS
ID : RF1 NS113636
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM141804
Pays : United States

Informations de copyright

Copyright © 2023 Elsevier Ltd. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

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Auteurs

Gemechu Mekonnen (G)

Program in Cellular Molecular Developmental Biology and Biophysics, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA.

Nathalie Djaja (N)

Program in Cellular Molecular Developmental Biology and Biophysics, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA.

Xincheng Yuan (X)

Program in Cellular Molecular Developmental Biology and Biophysics, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA.

Sua Myong (S)

Program in Cellular Molecular Developmental Biology and Biophysics, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA; Department of Biophysics, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA. Electronic address: smyong1@jhu.edu.

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Classifications MeSH