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A more recent version of this article appeared on December 1, 2004
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Submitted on August 18, 2004
Accepted on September 8, 2004
Division of Rheumatology, Immunology and Allergy, Brigham and Women’s Hospital, Boston, MA 02115
Monitoring Editor: Marvin P. Wickens
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 (RRMs) 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 which 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 molecular chaperone HSP70; resistance to protease digestion; sequestration of HSP27, HSP40 and HSP70; and induction of HSP70, a feedback regulator of PRD disaggregation. Substitution of the PRD with the aggregation domain of a yeast prion, SUP35-NM, reconstitutes SG assembly, confirming that a prion domain can mediate the assembly of SGs. MEFs lacking TIA-1 exhibit impaired ability to form SGs, although they exhibit normal phosphorylation of eIF2
in response to arsenite. Our results reveal that prion-like aggregation of TIA-1 regulates SG formation downstream of eIF2 phosphorylation in response to stress.
Present address: Renal Section, EBRC 504, Boston University Medical Center, 650 Albany Street, Boston, MA 02118.
*Corresponding author.
E-mail: nkedersha{at}rics.bwh.harvard.edu
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