한빛사논문
- 조회177
Sean R Millar 1, Jie Qi Huang 1, Karl J Schreiber 2, Yi-Cheng Tsai 1, Jiyun Won 3, Jianping Zhang 4, Alan M Moses 3,5,6, Ji-Young Youn 1,2
1Department of Molecular Genetics, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
2Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada.
3Department of Cell & Systems Biology, University of Toronto, Toronto, Ontario M5S 3B2, Canada.
4Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario M5G 1X5, Canada.
5Department of Computer Science, University of Toronto, Toronto, Ontario M5T 3A1, Canada.
6The Centre for the Analysis of Genome Evolution and Function, University of Toronto, Toronto, Ontario M5S 3B2, Canada.
*Corresponding author: Ji-Young Youn
Abstract
Stress granules (SGs) are cytosolic biomolecular condensates that form in response to cellular stress. Weak, multivalent interactions between their protein and RNA constituents drive their rapid, dynamic assembly through phase separation coupled to percolation. Though a consensus model of SG function has yet to be determined, their perceived implication in cytoprotective processes (e.g., antiviral responses and inhibition of apoptosis) and possible role in the pathogenesis of various neurodegenerative diseases (e.g., amyotrophic lateral sclerosis and frontotemporal dementia) have drawn great interest. Consequently, new studies using numerous cell biological, genetic, and proteomic methods have been performed to unravel the mechanisms underlying SG formation, organization, and function and, with them, a more clearly defined SG proteome. Here, we provide a consensus SG proteome through literature curation and an update of the user-friendly database RNAgranuleDB to version 2.0 (http://rnagranuledb.lunenfeld.ca/). With this updated SG proteome, we use next-generation phase separation prediction tools to assess the predisposition of SG proteins for phase separation and aggregation. Next, we analyze the primary sequence features of intrinsically disordered regions (IDRs) within SG-resident proteins. Finally, we review the protein- and RNA-level determinants, including post-translational modifications (PTMs), that regulate SG composition and assembly/disassembly dynamics.
논문정보
- Review Paper
- 2023년 01월 (BRIC 등록일 2023-03-17)
- 국외 연구진
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