Flipping the switch

Biomolecular condensates form and dissolve in response to a wide range of signals. A new study reports a solubility-based phosphoproteome-profiling approach, which uncovers the extensive role of phosphorylation in regulating protein partitioning into condensates across the human proteome.

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Bibliographic Details
Published in:	Nature chemical biology Vol. 18; no. 10; pp. 1041 - 1042
Main Authors:	Rizzolo, Kamran, Mitrea, Diana M.
Format:	Journal Article
Language:	English
Published:	New York Nature Publishing Group US 01-10-2022 Nature Publishing Group
Subjects:	631/337/386 631/92/458 631/92/475 Biochemical Engineering Biochemistry Biology Bioorganic Chemistry Cell Biology Chemistry Chemistry and Materials Science Chemistry/Food Science Condensates Enzymes Kinases News & Views news-and-views Phosphorylation Proteins Proteomes
Online Access:	Get full text
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Summary:	Biomolecular condensates form and dissolve in response to a wide range of signals. A new study reports a solubility-based phosphoproteome-profiling approach, which uncovers the extensive role of phosphorylation in regulating protein partitioning into condensates across the human proteome.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1552-4450 1552-4469
DOI:	10.1038/s41589-022-01075-7