The involvement of stress granules in aging and aging-associated diseases

被引:77
作者
Cao, Xiuling [1 ]
Jin, Xuejiao [1 ]
Liu, Beidong [1 ,2 ,3 ]
机构
[1] Zhejiang A&F Univ, Sch Forestry & Biotechnol, State Key Lab Subtrop Silviculture, Hangzhou, Peoples R China
[2] Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden
[3] Univ Gothenburg, Fac Sci, Ctr Large Scale Cell Based Screening, Gothenburg, Sweden
基金
中国国家自然科学基金;
关键词
aging; aging-associated diseases; nonmembrane assemblies; proteostasis; RNA-binding proteins; stress granules; FRONTOTEMPORAL LOBAR DEGENERATION; RNA-BINDING PROTEIN; AGE-RELATED-CHANGES; LIQUID PHASE-SEPARATION; LOW-COMPLEXITY DOMAINS; PRION-LIKE DOMAINS; MESSENGER-RNA; LIFE-SPAN; HEXANUCLEOTIDE REPEAT; TRANSLATIONAL CONTROL;
D O I
10.1111/acel.13136
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Stress granules (SGs) are nonmembrane assemblies formed in cells in response to stress conditions. SGs mainly contain untranslated mRNA and a variety of proteins. RNAs and scaffold proteins with intrinsically disordered regions or RNA-binding domains are essential for the assembly of SGs, and multivalent macromolecular interactions among these components are thought to be the driving forces for SG assembly. The SG assembly process includes regulation through post-translational modification and involvement of the cytoskeletal system. During aging, many intracellular bioprocesses become disrupted by factors such as cellular environmental changes, mitochondrial dysfunction, and decline in the protein quality control system. Such changes could lead to the formation of aberrant SGs, as well as alterations in their maintenance, disassembly, and clearance. These aberrant SGs might in turn promote aging and aging-associated diseases. In this paper, we first review the latest progress on the molecular mechanisms underlying SG assembly and SG functioning under stress conditions. Then, we provide a detailed discussion of the relevance of SGs to aging and aging-associated diseases.
引用
收藏
页数:20
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共 232 条
[1]   Membrane-bound organelles versus membrane-less compartments and their control of anabolic pathways in Drosophila [J].
Aguilera-Gomez, Angelica ;
Rabouille, Catherine .
DEVELOPMENTAL BIOLOGY, 2017, 428 (02) :310-317
[2]   Axonal Transport of TDP-43 mRNA Granules Is Impaired by ALS-Causing Mutations [J].
Alami, Nael H. ;
Smith, Rebecca B. ;
Carrasco, Monica A. ;
Williams, Luis A. ;
Winborn, Christina S. ;
Han, Steve S. W. ;
Kiskinis, Evangelos ;
Winborn, Brett ;
Freibaum, Brian D. ;
Kanagaraj, Anderson ;
Clare, Alison J. ;
Badders, Nisha M. ;
Bilican, Bilada ;
Chaum, Edward ;
Chandran, Siddharthan ;
Shaw, Christopher E. ;
Eggan, Kevin C. ;
Maniatis, Tom ;
Taylor, J. Paul .
NEURON, 2014, 81 (03) :536-543
[3]   Liquid-Liquid Phase Separation in Disease [J].
Alberti, Simon ;
Dormann, Dorothee .
ANNUAL REVIEW OF GENETICS, VOL 53, 2019, 53 :171-+
[4]   Are aberrant phase transitions a driver of cellular aging? [J].
Alberti, Simon ;
Hyman, Anthony A. .
BIOESSAYS, 2016, 38 (10) :959-968
[5]   A Systematic Survey Identifies Prions and Illuminates Sequence Features of Prionogenic Proteins [J].
Alberti, Simon ;
Halfmann, Randal ;
King, Oliver ;
Kapila, Atul ;
Lindquist, Susan .
CELL, 2009, 137 (01) :146-158
[6]   Protein quality control and elimination of protein waste: The role of the ubiquitin-proteasome system [J].
Amm, Ingo ;
Sommer, Thomas ;
Wolf, Dieter H. .
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 2014, 1843 (01) :182-196
[7]   TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis [J].
Arai, Tetsuaki ;
Hasegawa, Masato ;
Akiyama, Haruhiko ;
Ikeda, Kenji ;
Nonaka, Takashi ;
Mori, Hiroshi ;
Mann, David ;
Tsuchiya, Kuniaki ;
Yoshida, Marl ;
Hashizume, Yoshio ;
Oda, Tatsuro .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2006, 351 (03) :602-611
[8]   Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways [J].
Arimoto, Kyoko ;
Fukuda, Hiroyuki ;
Imajoh-Ohmi, Shinobu ;
Saito, Haruo ;
Takekawa, Mutsuhiro .
NATURE CELL BIOLOGY, 2008, 10 (11) :1324-U167
[9]   DYNAMIC CHANGES IN THE STRUCTURE AND INTRACELLULAR LOCALE OF THE MAMMALIAN LOW-MOLECULAR-WEIGHT HEAT-SHOCK PROTEIN [J].
ARRIGO, AP ;
SUHAN, JP ;
WELCH, WJ .
MOLECULAR AND CELLULAR BIOLOGY, 1988, 8 (12) :5059-5071
[10]  
Aumiller WM, 2016, NAT CHEM, V8, P129, DOI [10.1038/NCHEM.2414, 10.1038/nchem.2414]