Jared A.M. Bard

ArticleVolume 85, Issue 23p4393-4409.e11Open access 1Graduate Program in Biophysical Sciences, The University of Chicago, Chicago, IL, USA 2Interdisciplinary Scientist Training Program, The University of Chicago, Chicago, IL, USA 3Department of Biology, Texas A&M University, College Station, TX, USA 4Department of Biochemistry & Molecular Biology, The University of Chicago, Chicago, IL, USA 5Department of Molecular Genetics & Cell Biology, The University of Chicago, Chicago, IL, USA 6Fox...

Abstract Stress-induced condensation of mRNA and proteins into stress granules is conserved across eukaryotes, yet the function, formation mechanisms, and relation to well-studied conserved transcriptional responses remain largely unresolved. Stress-induced exposure of ribosome-free mRNA following translational shutoff is thought to cause condensation by allowing new multivalent RNA-dependent interactions, with RNA length and associated interaction capacity driving increased condensation.

Summary Stress-induced condensation of mRNA and protein into massive cytosolic clusters is conserved across eukaryotes. Known as stress granules when visible by imaging, these structures remarkably have no broadly accepted biological function, mechanism of formation or dispersal, or even molecular composition.