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TIA-1 Is a Functional Prion-Like Protein
Author(s) -
Joseph B. Rayman,
Eric R. Kandel
Publication year - 2016
Publication title -
cold spring harbor perspectives in biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.011
H-Index - 173
ISSN - 1943-0264
DOI - 10.1101/cshperspect.a030718
Subject(s) - stress granule , biology , protein aggregation , rna , prion protein , immune system , microbiology and biotechnology , granule (geology) , rna binding protein , function (biology) , disease , neuroscience , computational biology , biochemistry , genetics , messenger rna , translation (biology) , gene , medicine , paleontology , pathology
Prions are self-propagating protein conformations that are traditionally regarded as agents of neurodegenerative disease in animals. However, it has become evident that prion-like aggregation of endogenous proteins can also occur under normal physiological conditions (e.g., during memory storage or activation of the immune response). In this review, we focus on the functional prion-related protein TIA-1, an RNA-binding protein that is involved in multiple aspects of RNA metabolism but is best understood in terms of its role in stress granule assembly during the cellular stress response. We propose that stress granule formation provides a useful conceptual framework with which to address the positive role of TIA-1 prion-like aggregation. Elucidating the function of TIA-1 prion-like aggregation will advance our understanding of how prion-based molecular switches are used in normal physiological settings.

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