Phosphorylation Leads the Way for Protein Aggregate Disassembly

Steven Boeynaems; Aaron D Gitler

doi:10.1016/j.devcel.2018.04.017

Phosphorylation Leads the Way for Protein Aggregate Disassembly

Dev Cell. 2018 May 7;45(3):279-281. doi: 10.1016/j.devcel.2018.04.017.

Authors

Steven Boeynaems¹, Aaron D Gitler²

Affiliations

¹ Department of Genetics, Stanford University School of Medicine, Stanford, CA 94305, USA.
² Department of Genetics, Stanford University School of Medicine, Stanford, CA 94305, USA. Electronic address: [email protected].

PMID: 29738705
DOI: 10.1016/j.devcel.2018.04.017

Abstract

Protein aggregation can be beneficial, with important biological functions, but must be somehow controlled. In this issue of Developmental Cell, Carpenter et al. (2018) uncover how a solid-like supermolecular protein assembly that regulates yeast meiosis is disassembled through phosphorylation of a disordered prion-like domain to control the timing of meiotic progression.

Publication types

Comment

MeSH terms

Cell Cycle Proteins
Meiosis*
Phosphorylation
Protein Aggregates*
Saccharomyces cerevisiae

Substances

Cell Cycle Proteins
Protein Aggregates