Mechanistic insights into mammalian stress granule dynamics.
The accumulation of stalled translation preinitiation complexes (PICs) mediates the condensation of stress granules (SGs). Interactions between prion-related domains and intrinsically disordered protein regions found in SG-nucleating proteins promote the condensation of ribonucleoproteins into SGs. We propose that PIC components, especially 40S ribosomes and mRNA, recruit nucleators that trigger SG condensation. With resolution of stress, translation reinitiation reverses this process and SGs disassemble. By cooperatively modulating the assembly and disassembly of SGs, ribonucleoprotein condensation can influence the survival and recovery of cells exposed to unfavorable environmental conditions.
Division of Rheumatology, Immunology, and Allergy, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
Marc D
http://orcid.org/0000-0002-7373-0341
MD
Panas
Division of Rheumatology, Immunology, and Allergy, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
Pavel
P
Ivanov
Division of Rheumatology, Immunology, and Allergy, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115 panderson@rics.bwh.harvard.edu.
Paul
http://orcid.org/0000-0001-5349-281X
P
Anderson
D000818:Animals; D003594:Cytoplasmic Granules / Q000378:metabolism*; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000378:metabolism; D008322:Mammals / Q000378:metabolism*; D008954:Models, Biological; D012269:Ribosomal Proteins / Q000378:metabolism; D013312:Stress, Physiological
D064267:Intrinsically Disordered Proteins; D012269:Ribosomal Proteins