Stress Granule Assembly Is Mediated by Prion-like Aggregation of TIA-1
Indexed incrossrefpubmed
Abstract
TIA-1 is an RNA binding protein that promotes the assembly of stress granules (SGs), discrete cytoplasmic inclusions into which stalled translation initiation complexes are dynamically recruited in cells subjected to environmental stress. The RNA recognition motifs of TIA-1 are linked to a glutamine-rich prion-related domain (PRD). Truncation mutants lacking the PRD domain do not induce spontaneous SGs and are not recruited to arsenite-induced SGs, whereas the PRD forms aggregates that are recruited to SGs in low-level-expressing cells but prevent SG assembly in high-level-expressing cells. The PRD of TIA-1 exhibits many characteristics of prions: concentration-dependent aggregation that is inhibited by the…
Citation impact
996
total citations
- FWCI
- 7.11
- Percentile
- 100%
- References
- 61
Citations per year
Authors
7Topics & keywords
Topics
Keywords
- Stress granule
- Biology
- Cell biology
- Phosphorylation
- Chaperone (clinical)
- Mutant
- RNA
- Hsp70
UN Sustainable Development Goals
- Life in Land
No related works found for this paper.