TIA-1 Is a Functional Prion-Like Protein
نویسندگان
چکیده
منابع مشابه
Stress granule assembly is mediated by prion-like aggregation of TIA-1.
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 spontan...
متن کاملIs tau a prion-like protein?
It has been over a quarter century since the discovery in the mid-1980s that the paired helical filaments of neurofibrillary tangles were made up of abnormally hyperphosphorylated tau. A decade earlier tau had been first isolated from porcine brain as a heat stable protein essential for microtubule assembly. The following years clearly established tau as a microtubule-associated protein that un...
متن کاملDisease Transmission by Misfolded Prion-Protein Isoforms, Prion-Like Amyloids, Functional Amyloids and the Central Dogma.
In 1982, the term "prions" (proteinaceous infectious particles) was coined to specify a new principle of infection. A misfolded isoform of a cellular protein has been described as the causative agent of a fatal neurodegenerative disease. At the beginning of prion research scientists assumed that the infectious agent causing transmissible spongiform encephalopathy (TSE) was a virus, but some unc...
متن کاملIdentification and functional characterization of a TIA-1-related nucleolysin.
We recently reported the molecular cloning of a cytotoxic granule-associated RNA-binding protein designated TIA-1. The ability of recombinant TIA-1 to induce DNA fragmentation in permeabilized cells suggested that this protein is the granule component responsible for inducing apoptosis in cytolytic lymphocyte (CTL) targets. Here we report the characterization of a cDNA encoding a TIA-1-related ...
متن کاملRecent progress in prion and prion-like protein aggregation.
Prion diseases and prion-like protein misfolding diseases involve the accumulation of abnormally aggregated forms of the normal host proteins, such as prion protein and Tau protein. These proteins are special because of their self-duplicating and transmissible characteristics. Such abnormally aggregated proteins mainly formed in neurons, cause the neurons dysfunction, and finally lead to invari...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Cold Spring Harbor Perspectives in Biology
سال: 2016
ISSN: 1943-0264
DOI: 10.1101/cshperspect.a030718