Stress granules articles from across Nature Portfolio

Biomolecular condensates are non-membrane-encapsulated compartments that control various biological processes. Recent studies have revealed that condensates change in response to stimuli and over time. This Review discusses the heterogeneity and composition changes of nuclear and cytoplasmic condensates, their regulation and how the changes affect cellular biochemical reactions.

Here, the authors unveil the evolutionary conservation of lysine-rich IDRs of snoRNPs that mediate both efficient rRNA modification during active ribosome production and nucleolar compaction when ribosome synthesis declines and snoRNPs accumulate in latent state.

ZO-1, a cell junction protein, is essential for angiogenesis. Here the authors identify in endothelial cells unexpected associations of ZO-1 with stress granule proteins, such as YB-1, that are crucial for cytoprotection, implicating the ZO-1-YB-1 interaction in angiogenesis.

Different environmental stressors induce different subtypes of stress granules (SGs), and each of them presumably have distinct functions. Here the authors provide a framework for understanding the compositional and functional heterogeneity of SGs, and see that TRIM25 mainly associates with anti-viral SGs.

Cells must respond to environmental changes. In three fungal species adapted to different temperatures, cellular responses are conserved yet tuned to each organism’s thermal niche, including the formation of adaptive biomolecular condensates.

The cell interior is organized by diverse membrane-less condensates. Here, the authors reveal that the densities of certain condensates are surprisingly low, similar to the surrounding protoplasm and driven by cellular RNA as well as the crowded milieu.

A calcium-dependent pathway induces stress granule formation and promotes cell survival following lysosomal damage.

During cellular stresses, the mRNA internal 7-methylguanosine (m⁷G) modification is bound by QKI-7, which regulates the stability and/or translation of the mRNAs by sequestering them in stress granules.

The RNA-binding proteins RBGD2 and RBGD4 improve resistance to heat stress in plants by phase separating into heat-induced stress granules.

Cells respond to stimuli by reorganizing their contents into subcellular structures. New research demonstrates that yeast pyruvate kinase Cdc19 interacts with fructose-1,6-bisphosphate to coordinate disassembly of stress granules. These findings reveal how proteins can directly sense the cellular energy state to facilitate adaptive reorganization.