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Kyota, Y.

Publications and source records attributed to Kyota, Y..

2 recordsLinked to original sources

Stress Granules and FUS condensates recruit functionally distinct sets of RNAs

Cellular homeostasis relies on the organization of RNA and protein into membrane-less organelles. Stress granules (SGs) are well-known hubs for translational repression during cellular stress. Similar condensates formed by RNA-binding proteins such as FUS-- mutations in which cause amyotrophic lateral sclerosis (ALS)--remain poorly characterized relative to canonical SGs. Here, we develop Granule-seq, a microcapillary-based granule-resolved RNA sequencing approach, and demonstrate that SGs and FUS condensates are functionally distinct RNA compartments rather than variants of a unified granule class. Granules were individually aspirated, analyzed in small pooled sets, and validated through overlap with known SG components (794/2,759 genes, 28.8%, p < 0.001). Gene Ontology analysis revealed that G3BP-positive SGs sequester transcripts for stress responses and translational control, while FUS condensates are enriched for transcripts essential for synaptic function and neuronal development. Direct comparison showed that 63% of FUS-enriched and 82% of G3BP-enriched genes were granule-specific, with only 493 genes shared. Exploratory sequence analysis revealed modest contributions from compositional features, with functional identity providing primary selectivity. As a proof-of-concept study with limited biological replication, our results suggest that distinct granule identities are established through functionally specialized transcriptomes, a process that may be disrupted in ALS, and provide a framework for understanding RNA sorting. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=112 SRC="FIGDIR/small/726389v1_ufig1.gif" ALT="Figure 1"> View larger version (55K): org.highwire.dtl.DTLVardef@1378da9org.highwire.dtl.DTLVardef@35906borg.highwire.dtl.DTLVardef@9c7880org.highwire.dtl.DTLVardef@ab3b9d_HPS_FORMAT_FIGEXP M_FIG O_FLOATNOGraphic abstract.C_FLOATNO Granule-seq workflow and key findings.(Left) Individual cytoplasmic granules are isolated by microcapillary aspiration, pooled ([~]10 granules per replicate), and processed for RNA sequencing alongside total-cell input. (Middle) Venn diagram showing the overlap between FUS condensate-enriched (1,334 genes) and G3BP1 stress granule-enriched (2,759 genes) transcripts. FUS condensates preferentially recruit neuronal and synaptic transcripts; G3BP1 stress granules are enriched for stress-response and proteostasis transcripts. (Right) Two-step recruitment model: shared sequence features (long 3'UTR, GC-rich composition, stable RNA structure) provide permissiveness for granule entry (Step 1), while RBP interactome composition and functional context determine granule-type specificity (Step 2). C_FIG

molecular biology↗

hnRNPA2B1 Modulates Early TIA1 Recruitment into Stress Granules through an RNA-Dependent Assembly Mechanism

Stress granules (SGs) are dynamic, membrane-less assemblies that form in the cytoplasm in response to cellular stress. The ordered recruitment of proteins into SGs is fundamental to condensate composition and function, yet the molecular determinants of this ordered client recruitment remain incompletely understood. Using proximity photo-crosslinking proteomics, we identified heterogeneous nuclear ribonucleoprotein A2B1 (hnRNPA2B1) as a TIA1-proximal protein preferentially enriched in SGs under arsenite stress. Knockdown of hnRNPA2B1 preferentially delayed TIA1 enrichment in G3BP1-marked SGs at 20 min without affecting G3BP1 or the overall SG-positive cell fraction, and this phenotype showed directional rescue upon re-expression. In vitro droplet reconstitution assays with purified proteins revealed that hnRNPA2B1 and RNA cooperatively increased TIA1 incorporation capacity into G3BP1 condensates, an effect not attributable to changes in droplet size. Kinetic fitting identified hnRNPA2B1 + RNA as uniquely increasing the plateau amplitude of TIA1 recruitment (Cohens d = 1.62 versus RNA-alone condition). Coarse-grained simulations support an inside-out assembly model in which hnRNPA2B1 stabilizes the condensate core through homotypic interactions while RNA-bound TIA1 accumulates at the periphery. Together, these findings identify hnRNPA2B1 as a capacity-determining modulator of early TIA1 recruitment and provide a framework for understanding ordered protein assembly within stress granules.

cell biology↗