Advances in mass spectrometry to unravel the structure and function of protein condensates.
Journal
Nature protocols
ISSN: 1750-2799
Titre abrégé: Nat Protoc
Pays: England
ID NLM: 101284307
Informations de publication
Date de publication:
Dec 2023
Dec 2023
Historique:
received:
18
04
2023
accepted:
09
08
2023
medline:
7
12
2023
pubmed:
1
11
2023
entrez:
1
11
2023
Statut:
ppublish
Résumé
Membrane-less organelles assemble through liquid-liquid phase separation (LLPS) of partially disordered proteins into highly specialized microenvironments. Currently, it is challenging to obtain a clear understanding of the relationship between the structure and function of phase-separated protein assemblies, owing to their size, dynamics and heterogeneity. In this Perspective, we discuss recent advances in mass spectrometry (MS) that offer several promising approaches for the study of protein LLPS. We survey MS tools that have provided valuable insights into other insoluble protein systems, such as amyloids, and describe how they can also be applied to study proteins that undergo LLPS. On the basis of these recent advances, we propose to integrate MS into the experimental workflow for LLPS studies. We identify specific challenges and future opportunities for the analysis of protein condensate structure and function by MS.
Identifiants
pubmed: 37907762
doi: 10.1038/s41596-023-00900-0
pii: 10.1038/s41596-023-00900-0
doi:
Substances chimiques
Intrinsically Disordered Proteins
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
3653-3661Subventions
Organisme : Vetenskapsrådet (Swedish Research Council)
ID : 2019-01961
Organisme : Cancerfonden (Swedish Cancer Society)
ID : 22 2033
Organisme : Novo Nordisk Foundation Center for Basic Metabolic Research (NovoNordisk Foundation Center for Basic Metabolic Research)
ID : NNF19OC0055700
Organisme : Stiftelsen Olle Engkvist Byggmästare
ID : OE2022
Informations de copyright
© 2023. Springer Nature Limited.
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