Pathophysiology of stress granules: An emerging link to diseases (Review)
- Authors:
- Jihui Wang
- Yixia Gan
- Jian Cao
- Xuefen Dong
- Wei Ouyang
-
Affiliations: Department of Kinesiology and Human Sciences, College of Physical Education and Health Sciences, Zhejiang Normal University, Jinhua, Zhejiang 321004, P.R. China - Published online on: February 7, 2022 https://doi.org/10.3892/ijmm.2022.5099
- Article Number: 44
-
Copyright: © Wang et al. This is an open access article distributed under the terms of Creative Commons Attribution License.
This article is mentioned in:
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 |
 |
|
Ivanov P, Kedersha N and Anderson P: Stress granules and processing bodies in translational control. Cold Spring Harb Perspect Biol. 11:a0328132019. View Article : Google Scholar | |
|
Hentze MW, Castello A, Schwarzl T and Preiss T: A brave new world of RNA-binding proteins. Nat Rev Mol Cell Biol. 19:327–341. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Shin Y and Brangwynne CP: Liquid phase condensation in cell physiology and disease. Science. 357:eaaf43822017. View Article : Google Scholar : PubMed/NCBI | |
|
Riggs CL, Kedersha N, Ivanov P and Anderson P: Mammalian stress granules and P bodies at a glance. J Cell Sci. 133:jcs2424872020. View Article : Google Scholar : PubMed/NCBI | |
|
Heberle AM, Razquin Navas P, Langelaar-Makkinje M, Kasack K, Sadik A, Faessler E, Hahn U, Marx-Stoelting P, Opitz CA, Sers C, et al: The PI3K and MAPK/p38 pathways control stress granule assembly in a hierarchical manner. Life Sci Alliance. 2:e2018002572019. View Article : Google Scholar : | |
|
Golob-Schwarzl N, Krassnig S, Toeglhofer AM, Park YN, Gogg-Kamerer M, Vierlinger K, Schröder F, Rhee H, Schicho R, Fickert P and Haybaeck J: New liver cancer biomarkers: PI3K/AKT/mTOR pathway members and eukaryotic translation initiation factors. Eur J Cancer. 83:56–70. 2017. View Article : Google Scholar : PubMed/NCBI | |
|
Sfakianos AP, Mellor LE, Pang YF, Kritsiligkou P, Needs H, Abou-Hamdan H, Désaubry L, Poulin GB, Ashe MP and Whitmarsh AJ: The mTOR-S6 kinase pathway promotes stress granule assembly. Cell Death Differ. 25:1766–1780. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Onomoto K, Yoneyama M, Fung G, Kato H and Fujita T: Antiviral innate immunity and stress granule responses. Trends Immunol. 35:420–428. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
McCormick C and Khaperskyy DA: Translation inhibition and stress granules in the antiviral immune response. Nat Rev Immunol. 17:647–660. 2017. View Article : Google Scholar : PubMed/NCBI | |
|
Li Q, Leng K, Liu Y, Sun H, Gao J, Ren Q, Zhou T, Dong J and Xia J: The impact of hyperglycaemia on PKM2-mediated NLRP3 inflammasome/stress granule signalling in macrophages and its correlation with plaque vulnerability: An in vivo and in vitro study. Metabolism. 107:1542312020. View Article : Google Scholar : PubMed/NCBI | |
|
Herman AB, Silva Afonso M, Kelemen SE, Ray M, Vrakas CN, Burke AC, Scalia RG, Moore K and Autieri MV: Regulation of stress granule formation by inflammation, vascular injury, and atherosclerosis. Arterioscler Thromb Vasc Biol. 39:2014–2027. 2019. View Article : Google Scholar : PubMed/NCBI | |
|
Patel A, Lee HO, Jawerth L, Maharana S, Jahnel M, Hein MY, Stoynov S, Mahamid J, Saha S, Franzmann TM, et al: A Liquid-to-Solid phase transition of the ALS Protein FUS accelerated by disease mutation. Cell. 162:1066–1077. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Ramaswami M, Taylor JP and Parker R: Altered ribostasis: RNA-protein granules in degenerative disorders. Cell. 154:727–736. 2013. View Article : Google Scholar : PubMed/NCBI | |
|
Ambadipudi S, Biernat J, Riedel D, Mandelkow E and Zweckstetter M: Liquid-liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau. Nat Commu. 8:2752017. View Article : Google Scholar | |
|
Wegmann S, Eftekharzadeh B, Tepper K, Zoltowska KM, Bennett RE, Dujardin S, Laskowski PR, MacKenzie D, Kamath T, Commins C, et al: Tau protein liquid-liquid phase separation can initiate tau aggregation. EMBO J. 37:e980492018. View Article : Google Scholar : PubMed/NCBI | |
|
Kedersha N, Chen S, Gilks N, Li W, Miller IJ, Stahl J and Anderson P: Evidence that ternary complex (eIF2-GTP-tRNA(i) (Met))-deficient preinitiation complexes are core constituents of mammalian stress granules. Mol Biol Cell. 13:195–210. 2002. View Article : Google Scholar : PubMed/NCBI | |
|
Anderson P and Kedersha N: Visibly stressed: The role of eIF2, TIA-1, and stress granules in protein translation. Cell Stress Chaperones. 7:213–221. 2002. View Article : Google Scholar | |
|
Hofmann S, Kedersha N, Anderson P and Ivanov P: Molecular mechanisms of stress granule assembly and disassembly. Biochim Biophys Acta Mol Cell Res. 1868:1188762021. View Article : Google Scholar | |
|
Wolozin B and Ivanov P: Stress granules and neurodegeneration. Na Rev Neurosci. 20:649–666. 2019. View Article : Google Scholar | |
|
Jain S, Wheeler JR, Walters RW, Agrawal A, Barsic A and Parker R: ATPase-modulated stress granules contain a diverse proteome and substructure. Cell. 164:487–498. 2016. View Article : Google Scholar : PubMed/NCBI | |
|
Protter DSW and Parker R: Principles and properties of stress granules. Trends Cell Biol. 26:668–679. 2016. View Article : Google Scholar : PubMed/NCBI | |
|
Markmiller S, Soltanieh S, Server KL, Mak R, Jin W, Fang MY, Luo EC, Krach F, Yang D, Sen A, et al: Context-dependent and disease-specific diversity in protein interactions within stress granules. Cell. 172:590–604.e13. 2018. View Article : Google Scholar : | |
|
Kedersha N, Panas MD, Achorn CA, Lyons S, Tisdale S, Hickman T, Thomas M, Lieberman J, McInerney GM, Ivanov P and Anderson P: G3BP-Caprin1-USP10 complexes mediate stress granule condensation and associate with 40S subunits. J Cell Biol. 212:845–860. 2016. View Article : Google Scholar : PubMed/NCBI | |
|
Anderson P and Kedersha N: Stress granules: The Tao of RNA triage. Trends Biochem Sci. 33:141–150. 2008. View Article : Google Scholar : PubMed/NCBI | |
|
Kaehler C, Isensee J, Hucho T, Lehrach H and Krobitsch S: 5-fluorouracil affects assembly of stress granules based on RNA incorporation. Nucleic Acids Res. 42:6436–6447. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Fujimura K, Sasaki AT and Anderson P: Selenite targets eIF4E-binding protein-1 to inhibit translation initiation and induce the assembly of non-canonical stress granules. Nucleic Acids Res. 40:8099–8110. 2012. View Article : Google Scholar : PubMed/NCBI | |
|
Ohn T, Kedersha N, Hickman T, Tisdale S and Anderson P: A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly. Nat Cell Biol. 10:1224–1231. 2008. View Article : Google Scholar | |
|
Aulas A, Lyons SM, Fay MM, Anderson P and Ivanov P: Nitric oxide triggers the assembly of 'type II' stress granules linked to decreased cell viability. Cell Death Dis. 9:11292018. View Article : Google Scholar | |
|
Anderson P and Kedersha N: RNA granules. J Cell Biol. 172:803–808. 2006. View Article : Google Scholar : PubMed/NCBI | |
|
Huang C, Chen Y, Dai H, Zhang H, Xie M, Zhang H, Chen F, Kang X, Bai X and Chen Z: UBAP2L arginine methylation by PRMT1 modulates stress granule assembly. Cell Death Differ. 27:227–241. 2020. View Article : Google Scholar | |
|
Tsai WC, Gayatri S, Reineke LC, Sbardella G, Bedford MT and Lloyd RE: Arginine demethylation of G3BP1 promotes stress granule assembly. J Biol Chemistry. 291:22671–22685. 2016. View Article : Google Scholar | |
|
Kedersha N and Anderson P: Stress granules: Sites of mRNA triage that regulate mRNA stability and translatability. Biochem Soc Trans. 30:963–969. 2002. View Article : Google Scholar : PubMed/NCBI | |
|
Mateju D, Eichenberger B, Voigt F, Eglinger J, Roth G and Chao JA: Single-molecule imaging reveals translation of mRNAs localized to stress granules. Cell. 183:1801–1812.e13. 2020. View Article : Google Scholar : PubMed/NCBI | |
|
Arimoto K, Fukuda H, Imajoh-Ohmi S, Saito H and Takekawa M: Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways. Nat Cell Biol. 10:1324–1332. 2008. View Article : Google Scholar : PubMed/NCBI | |
|
Park YJ, Choi DW, Cho SW, Han J, Yang S and Choi CY: Stress granule formation attenuates RACK1-mediated apoptotic cell death induced by morusin. Int J Mol Sci. 21:53602020. View Article : Google Scholar : | |
|
Panas MD, Ivanov P and Anderson P: Mechanistic insights into mammalian stress granule dynamics. J Cell Biol. 215:313–323. 2016. View Article : Google Scholar : | |
|
Tourrière H, Chebli K, Zekri L, Courselaud B, Blanchard JM, Bertrand E and Tazi J: The RasGAP-associated endoribonuclease G3BP assembles stress granules. J Cell Biol. 160:823–831. 2003. View Article : Google Scholar | |
|
Omer A, Patel D, Moran JL, Lian XJ, Di Marco S and Gallouzi IE: Autophagy and heat-shock response impair stress granule assembly during cellular senescence. Mech Ageing Dev. 192:1113822020. View Article : Google Scholar : PubMed/NCBI | |
|
Omer A, Barrera MC, Moran JL, Lian XJ, Di Marco S, Beausejour C and Gallouzi IE: G3BP1 controls the senescence-associated secretome and its impact on cancer progression. Nat Commun. 11:49792020. View Article : Google Scholar : PubMed/NCBI | |
|
Coppé JP, Desprez PY, Krtolica A and Campisi J: The senescence-associated secretory phenotype: The dark side of tumor suppression. Annu Rev Pathol. 5:99–118. 2010. View Article : Google Scholar : PubMed/NCBI | |
|
Anderson P, Kedersha N and Ivanov P: Stress granules, P-bodies and cancer. Biochim Biophys Acta. 1849:861–870. 2015. View Article : Google Scholar : | |
|
El-Naggar AM and Sorensen PH: Translational control of aberrant stress responses as a hallmark of cancer. J Pathol. 244:650–666. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Vilas-Boas Fde A, da Silva AM, de Sousa LP, Lima KM, Vago JP, Bittencourt LF, Dantas AE, Gomes DA, Vilela MC, Teixeira MM and Barcelos LS: Impairment of stress granule assembly via inhibition of the eIF2alpha phosphorylation sensitizes glioma cells to chemotherapeutic agents. J Neurooncol. 127:253–260. 2016. View Article : Google Scholar : PubMed/NCBI | |
|
Fournier MJ, Gareau C and Mazroui R: The chemotherapeutic agent bortezomib induces the formation of stress granules. Cancer Cell Int. 10:122010. View Article : Google Scholar : | |
|
Gao X, Jiang L, Gong Y, Chen X, Ying M, Zhu H, He Q, Yang B and Cao J: Stress granule: A promising target for cancer treatment. Br J Pharmacol. 176:4421–4433. 2019. View Article : Google Scholar : PubMed/NCBI | |
|
Khan FH, Dervan E, Bhattacharyya DD, McAuliffe JD, Miranda KM and Glynn SA: The role of nitric oxide in cancer: Master regulator or NOt? Int J Mol Sci. 21:93932020. View Article : Google Scholar : | |
|
Alam U and Kennedy D: G3BP1 and G3BP2 regulate translation of interferon-stimulated genes: IFITM1, IFITM2 and IFITM3 in the cancer cell line MCF7. Mol Cell Biochem. 459:189–204. 2019. View Article : Google Scholar | |
|
Gupta N, Badeaux M, Liu Y, Naxerova K, Sgroi D, Munn LL, Jain RK and Garkavtsev I: Stress granule-associated protein G3BP2 regulates breast tumor initiation. Proc Natl Acad Sci USA. 114:1033–1038. 2017. View Article : Google Scholar : PubMed/NCBI | |
|
Somasekharan SP, El-Naggar A, Leprivier G, Cheng H, Hajee S, Grunewald TG, Zhang F, Ng T, Delattre O, Evdokimova V, et al: YB-1 regulates stress granule formation and tumor progression by translationally activating G3BP1. J Cell Biol. 208:913–929. 2015. View Article : Google Scholar : | |
|
Ramachandran B, Stabley JN, Cheng SL, Behrmann AS, Gay A, Li L, Mead M, Kozlitina J, Lemoff A, Mirzaei H, et al: A GTPase-activating protein-binding protein (G3BP1)/antiviral protein relay conveys arteriosclerotic Wnt signals in aortic smooth muscle cells. J Biol Chem. 293:7942–7968. 2018. View Article : Google Scholar : | |
|
Schneider JW, Oommen S, Qureshi MY, Goetsch SC, Pease DR, Sundsbak RS, Guo W, Sun M, Sun H, Kuroyanagi H, et al: Dysregulated ribonucleoprotein granules promote cardiomyopathy in RBM20 gene-edited pigs. Nat Med. 26:1788–1800. 2020. View Article : Google Scholar | |
|
Smit M, Coetzee AR and Lochner A: The pathophysiology of myocardial ischemia and perioperative myocardial infarction. J Cardiothorac Vasc Anesth. 34:2501–2512. 2020. View Article : Google Scholar | |
|
Garikipati VNS, Verma SK, Cheng Z, Liang D, Truongcao MM, Cimini M, Yue Y, Huang G, Wang C, Benedict C, et al: Circular RNA CircFndc3b modulates cardiac repair after myocardial infarction via FUS/VEGF-A axis. Nat Commun. 10:43172019. View Article : Google Scholar : PubMed/NCBI | |
|
Mahboubi H and Stochaj U: Cytoplasmic stress granules: Dynamic modulators of cell signaling and disease. Biochim Biophys Acta Mol Basis Dis. 1863:884–895. 2017. View Article : Google Scholar | |
|
Yoneyama M, Jogi M and Onomoto K: Regulation of antiviral innate immune signaling by stress-induced RNA granules. J Biochem. 159:279–286. 2016.PubMed/NCBI | |
|
Xu S, Chen D, Chen D, Hu Q, Zhou L, Ge X, Han J, Guo X and Yang H: Pseudorabies virus infection inhibits stress granules formation via dephosphorylating eIF2α. Vet Microbiol. 247:1087862020. View Article : Google Scholar | |
|
Khong A, Kerr CH, Yeung CHL, Keatings K, Nayak A, Allan DW and Jan E: Disruption of stress granule formation by the multifunctional cricket paralysis virus 1A protein. J Virol. 91:e01779–16. 2017. View Article : Google Scholar : | |
|
Visser LJ, Medina GN, Rabouw HH, de Groot RJ, Langereis MA, de Los Santos T and van Kuppeveld FJM: Foot-and-Mouth disease virus leader protease cleaves G3BP1 and G3BP2 and inhibits stress granule formation. J Virol. 93:e00922–18. 2019. View Article : Google Scholar : | |
|
Dougherty JD, Tsai WC and Lloyd RE: Multiple poliovirus proteins repress cytoplasmic RNA granules. Viruses. 7:6127–6140. 2015. View Article : Google Scholar | |
|
Yang X, Hu Z, Fan S, Zhang Q, Zhong Y, Guo D, Qin Y and Chen M: Picornavirus 2A protease regulates stress granule formation to facilitate viral translation. PLoS Pathog. 14:e10069012018. View Article : Google Scholar : PubMed/NCBI | |
|
Le Sage V, Cinti A, McCarthy S, Amorim R, Rao S, Daino GL, Tramontano E, Branch DR and Mouland AJ: Ebola virus VP35 blocks stress granule assembly. Virology. 502:73–83. 2017. View Article : Google Scholar | |
|
Savastano A, Ibáñez de Opakua A, Rankovic M and Zweckstetter M: Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates. Nat Commun. 11:60412020. View Article : Google Scholar : PubMed/NCBI | |
|
Wang J, Shi C, Xu Q and Yin H: SARS-CoV-2 nucleocapsid protein undergoes liquid-liquid phase separation into stress granules through its N-terminal intrinsically disordered region. Cell Discov. 7:52021. View Article : Google Scholar : PubMed/NCBI | |
|
Lu S, Ye Q, Singh D, Cao Y, Diedrich JK, Yates JR III, Villa E, Cleveland DW and Corbett KD: The SARS-CoV-2 nucleocapsid phosphoprotein forms mutually exclusive condensates with RNA and the membrane-associated M protein. Nat Commun. 12:5022021. View Article : Google Scholar : PubMed/NCBI | |
|
Prasad K, Alasmari AF, Ali N, Khan R, Alghamdi A and Kumar V: Insights into the SARS-CoV-2-Mediated alteration in the stress granule protein regulatory networks in humans. Pathogens. 10:14592021. View Article : Google Scholar : PubMed/NCBI | |
|
Thoms M, Buschauer R, Ameismeier M, Koepke L, Denk T, Hirschenberger M, Kratzat H, Hayn M, Mackens-Kiani T, Cheng J, et al: Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2. Science. 369:1249–1255. 2020. View Article : Google Scholar : PubMed/NCBI | |
|
Shi M, Wang L, Fontana P, Vora S, Zhang Y, Fu TM, Lieberman J and Wu H: SARS-CoV-2 Nsp1 suppresses host but not viral translation through a bipartite mechanism. bioRxiv. 2020:3029012020. | |
|
Schubert K, Karousis ED, Jomaa A, Scaiola A, Echeverria B, Gurzeler LA, Leibundgut M, Thiel V, Mühlemann O and Ban N: SARS-CoV-2 Nsp1 binds the ribosomal mRNA channel to inhibit translation. Nat Struct Mol Biol. 27:959–966. 2020. View Article : Google Scholar : PubMed/NCBI | |
|
Nakagawa K, Narayanan K, Wada M and Makino S: Inhibition of stress granule formation by middle east respiratory syndrome coronavirus 4a accessory protein facilitates viral translation, leading to efficient virus replication. J Virol. 92:e00902–18. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Callaway E: Heavily mutated omicron variant puts scientists on alert. Nature. 600:212021. View Article : Google Scholar : PubMed/NCBI | |
|
Dudman J and Qi X: Stress granule dysregulation in amyotrophic lateral sclerosis. Front Cell Neurosci. 14:5985172020. View Article : Google Scholar : PubMed/NCBI | |
|
Anderson EN, Gochenaur L, Singh A, Grant R, Patel K, Watkins S, Wu JY and Pandey UB: Traumatic injury induces stress granule formation and enhances motor dysfunctions in ALS/FTD models. Hum Mol Genet. 27:1366–1381. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Ayuso MI, Martínez-Alonso E, Regidor I and Alcázar A: Stress granule induction after brain ischemia is independent of eukaryotic translation initiation factor (eIF) 2α phosphorylation and is correlated with a decrease in eIF4B and eIF4E proteins. J Biol Chemistry. 291:27252–27264. 2016. View Article : Google Scholar | |
|
Correia AS, Patel P, Dutta K and Julien JP: Inflammation induces TDP-43 mislocalization and aggregation. PLoS One. 10:e01402482015. View Article : Google Scholar : PubMed/NCBI | |
|
Cao X, Jin X and Liu B: The involvement of stress granules in aging and aging-associated diseases. Aging Cell. 19:e131362020. View Article : Google Scholar : PubMed/NCBI | |
|
Cruz A, Verma M and Wolozin B: The Pathophysiology of tau and stress granules in disease. Adv Exp Med Biol. 1184:359–372. 2019. View Article : Google Scholar | |
|
Webber CJ, Lei SE and Wolozin B: The pathophysiology of neurodegenerative disease: Disturbing the balance between phase separation and irreversible aggregation. Prog Mol Biol Transl Sci. 174:187–223. 2020. View Article : Google Scholar : PubMed/NCBI | |
|
Rozpędek-Kamińska W, Siwecka N, Wawrzynkiewicz A, Wojtczak R, Pytel D, Diehl JA and Majsterek I: The PERK-dependent molecular mechanisms as a novel therapeutic target for neurodegenerative diseases. Int J Mol Sci. 21:21082020. View Article : Google Scholar | |
|
Ma T, Trinh MA, Wexler AJ, Bourbon C, Gatti E, Pierre P, Cavener DR and Klann E: Suppression of eIF2α kinases alleviates Alzheimer's disease-related plasticity and memory deficits. Nat Neurosci. 16:1299–1305. 2013. View Article : Google Scholar : PubMed/NCBI | |
|
Kim HJ, Raphael AR, LaDow ES, McGurk L, Weber RA, Trojanowski JQ, Lee VM, Finkbeiner S, Gitler AD and Bonini NM: Therapeutic modulation of eIF2α phosphorylation rescues TDP-43 toxicity in amyotrophic lateral sclerosis disease models. Nat Genet. 46:152–160. 2014. View Article : Google Scholar | |
|
Banani SF, Lee HO, Hyman AA and Rosen MK: Biomolecular condensates: Organizers of cellular biochemistry. Nat Rev Mol Cell Biol. 18:285–298. 2017. View Article : Google Scholar : PubMed/NCBI | |
|
Flores BN, Li X, Malik AM, Martinez J, Beg AA and Barmada SJ: An intramolecular salt bridge linking TDP43 RNA binding, protein stability, and TDP43-dependent neurodegeneration. Cell Rep. 27:1133–1150.e8. 2019. View Article : Google Scholar : PubMed/NCBI | |
|
Archbold HC, Jackson KL, Arora A, Weskamp K, Tank EM, Li X, Miguez R, Dayton RD, Tamir S, Klein RL and Barmada SJ: TDP43 nuclear export and neurodegeneration in models of amyotrophic lateral sclerosis and frontotemporal dementia. Sci Rep. 8:46062018. View Article : Google Scholar : | |
|
Suk TR and Rousseaux MWC: The role of TDP-43 mislocalization in amyotrophic lateral sclerosis. Mol Neurodegener. 15:452020. View Article : Google Scholar : PubMed/NCBI | |
|
Tomé SO, Vandenberghe R, Ospitalieri S, Van Schoor E, Tousseyn T, Otto M, von Arnim CAF and Thal DR: Distinct molecular patterns of TDP-43 pathology in Alzheimer's disease: Relationship with clinical phenotypes. Acta Neuropathol Commun. 8:612020. View Article : Google Scholar | |
|
Vanderweyde T, Apicco DJ, Youmans-Kidder K, Ash PEA, Cook C, Lummertz da Rocha E, Jansen-West K, Frame AA, Citro A, Leszyk JD, et al: Interaction of tau with the RNA-binding Protein TIA1 regulates tau pathophysiology and toxicity. Cell Rep. 15:1455–1466. 2016. View Article : Google Scholar : PubMed/NCBI | |
|
Apicco DJ, Ash PEA, Maziuk B, LeBlang C, Medalla M, Al Abdullatif A, Ferragud A, Botelho E, Ballance HI, Dhawan U, et al: Reducing the RNA binding protein TIA1 protects against tau-mediated neurodegeneration in vivo. Nat Neurosci. 21:72–80. 2018. View Article : Google Scholar | |
|
Gal J, Kuang L, Barnett KR, Zhu BZ, Shissler SC, Korotkov KV, Hayward LJ, Kasarskis EJ and Zhu H: ALS mutant SOD1 interacts with G3BP1 and affects stress granule dynamics. Acta Neuropathol. 132:563–576. 2016. View Article : Google Scholar : PubMed/NCBI | |
|
Sidibé H, Dubinski A and Vande Velde C: The multi-functional RNA-binding protein G3BP1 and its potential implication in neurodegenerative disease. J Neurochem. 157:944–962. 2021. View Article : Google Scholar | |
|
Gogia N, Sarkar A, Mehta AS, Ramesh N, Deshpande P, Kango-Singh M, Pandey UB and Singh A: Inactivation of Hippo and cJun-N-terminal Kinase (JNK) signaling mitigate FUS mediated neurodegeneration in vivo. Neurobio Dis. 140:1048372020. View Article : Google Scholar | |
|
Picchiarelli G, Demestre M, Zuko A, Been M, Higelin J, Dieterlé S, Goy MA, Mallik M, Sellier C, Scekic-Zahirovic J, et al: FUS-mediated regulation of acetylcholine receptor transcription at neuromuscular junctions is compromised in amyotrophic lateral sclerosis. Nat Neurosci. 22:1793–1805. 2019. View Article : Google Scholar : PubMed/NCBI | |
|
Fifita JA, Zhang KY, Galper J, Williams KL, McCann EP, Hogan AL, Saunders N, Bauer D, Tarr IS, Pamphlett R, et al: Genetic and pathological assessment of hnRNPA1, hnRNPA2/B1, and hnRNPA3 in familial and sporadic amyotrophic lateral sclerosis. Neurodegener Dis. 17:304–312. 2017. View Article : Google Scholar : PubMed/NCBI | |
|
Kim HJ, Kim NC, Wang YD, Scarborough EA, Moore J, Diaz Z, MacLea KS, Freibaum B, Li S, Molliex A, et al: Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multi-system proteinopathy and ALS. Nature. 495:467–473. 2013. View Article : Google Scholar : PubMed/NCBI | |
|
Montalbano M, McAllen S, Cascio FL, Sengupta U, Garcia S, Bhatt N, Ellsworth A, Heidelman EA, Johnson OD, Doskocil S and Kayed R: TDP-43 and tau oligomers in Alzheimer's disease, amyotrophic lateral sclerosis, and frontotemporal dementia. Neurobiol Dis. 146:1051302020. View Article : Google Scholar : PubMed/NCBI | |
|
Zhao M, Kim JR, van Bruggen R and Park J: RNA-binding proteins in amyotrophic lateral sclerosis. Mol Cells. 41:818–829. 2018.PubMed/NCBI | |
|
Mackenzie IR, Nicholson AM, Sarkar M, Messing J, Purice MD, Pottier C, Annu K, Baker M, Perkerson RB, Kurti A, et al: TIA1 mutations in amyotrophic lateral sclerosis and frontotemporal dementia promote phase separation and alter stress granule dynamics. Neuron. 95:808–816.e9. 2017. View Article : Google Scholar : PubMed/NCBI | |
|
Chew J, Gendron TF, Prudencio M, Sasaguri H, Zhang YJ, Castanedes-Casey M, Lee CW, Jansen-West K, Kurti A, Murray ME, et al: Neurodegeneration. C9ORF72 repeat expansions in mice cause TDP-43 pathology, neuronal loss, and behavioral deficits. Science. 348:1151–1154. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Chew J, Cook C, Gendron TF, Jansen-West K, Del Rosso G, Daughrity LM, Castanedes-Casey M, Kurti A, Stankowski JN, Disney MD, et al: Aberrant deposition of stress granule-resident proteins linked to C9orf72-associated TDP-43 proteinopathy. Mol Neurodegener. 14:92019. View Article : Google Scholar : | |
|
Chitiprolu M, Jagow C, Tremblay V, Bondy-Chorney E, Paris G, Savard A, Palidwor G, Barry FA, Zinman L, Keith J, et al: A complex of C9ORF72 and p62 uses arginine methylation to eliminate stress granules by autophagy. Nat Commun. 9:27942018. View Article : Google Scholar : PubMed/NCBI | |
|
Deng Z, Lim J, Wang Q, Purtell K, Wu S, Palomo GM, Tan H, Manfredi G, Zhao Y, Peng J, et al: ALS-FTLD-linked mutations of SQSTM1/p62 disrupt selective autophagy and NFE2L2/NRF2 anti-oxidative stress pathway. Autophagy. 16:917–931. 2020. View Article : Google Scholar : | |
|
Jiang Z, Belforte JE, Lu Y, Yabe Y, Pickel J, Smith CB, Je HS, Lu B and Nakazawa K: eIF2alpha Phosphorylation-dependent translation in CA1 pyramidal cells impairs hippocampal memory consolidation without affecting general translation. J Neurosci. 30:2582–2594. 2010. View Article : Google Scholar : PubMed/NCBI | |
|
Trinh MA, Ma T, Kaphzan H, Bhattacharya A, Antion MD, Cavener DR, Hoeffer CA and Klann E: The eIF2α kinase PERK limits the expression of hippocampal metabotropic glutamate receptor-dependent long-term depression. Learn Mem. 21:298–304. 2014. View Article : Google Scholar : | |
|
Hijioka M, Inden M, Yanagisawa D and Kitamura Y: DJ-1/PARK7: A new therapeutic target for neurodegenerative disorders. Biol Pharm Bull. 40:548–552. 2017. View Article : Google Scholar : PubMed/NCBI | |
|
Repici M, Hassanjani M, Maddison DC, Garção P, Cimini S, Patel B, Szegö ÉM, Straatman KR, Lilley KS, Borsello T, et al: The Parkinson's disease-linked protein DJ-1 associates with cytoplasmic mRNP granules during stress and neurodegeneration. Mol Neurobiol. 56:61–77. 2019. View Article : Google Scholar | |
|
Ma J, Wu R, Zhang Q, Wu JB, Lou J, Zheng Z, Ding JQ and Yuan Z: DJ-1 interacts with RACK1 and protects neurons from oxidative-stress-induced apoptosis. Biochem J. 462:489–497. 2014. View Article : Google Scholar |
