Aging-induced YTHDF aggregates impair mitochondrial function by trapping mitochondrial RNAs and suppressing their expression in the brain

Juan Zhang; Dingfeng Li; Keqiang He; Qiang Liu; Zhongwen Xie

doi:10.1093/procel/pwad041

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Protein Cell ›› 2024, Vol. 15 ›› Issue (2) : 149-155. DOI: 10.1093/procel/pwad041

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Aging-induced YTHDF aggregates impair mitochondrial function by trapping mitochondrial RNAs and suppressing their expression in the brain

Juan Zhang¹^,² ,
Dingfeng Li³ ,
Keqiang He⁴ ,
Qiang Liu³^,⁵^,⁶ ,
Zhongwen Xie²

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Juan Zhang, Dingfeng Li, Keqiang He, Qiang Liu, Zhongwen Xie. Aging-induced YTHDF aggregates impair mitochondrial function by trapping mitochondrial RNAs and suppressing their expression in the brain. Protein Cell, 2024, 15(2): 149‒155 https://doi.org/10.1093/procel/pwad041

References

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[1]	Chen L, Gao Y, Xu S et al. N6-methyladenosine reader YTHDF family in biological processes: structures, roles, and mechanisms. Front Immunol 2023;14:1162607. CrossRef Google scholar

[2]	Faitg J, Lacefield C, Davey T et al. 3D neuronal mitochondrial morphology in axons, dendrites, and somata of the aging mouse hippocampus. Cell Rep 2021;36:109509. CrossRef Google scholar

[3]	Gao Y, Pei G, Li D et al. Multivalent m(6)A motifs promote phase separation of YTHDF proteins. Cell Res 2019;29:767–769. CrossRef Google scholar

[4]	Grimm A, Eckert A. Brain aging and neurodegeneration: from a mitochondrial point of view. J Neurochem 2017;143:418–431. CrossRef Google scholar

[5]	Kelmer Sacramento E, Kirkpatrick JM, Mazzetto M et al. Reduced proteasome activity in the aging brain results in ribosome stoichiometry loss and aggregation. Mol Syst Biol 2020;16:e9596. CrossRef Google scholar

[6]	Lee A, Hirabayashi Y, Kwon SK et al. Emerging roles of mitochondria in synaptic transmission and neurodegeneration. Curr Opin Physiol 2018;3:82–93. CrossRef Google scholar

[7]	Pellegrini L, Scorrano L. A cut short to death: Parl and Opa1 in the regulation of mitochondrial morphology and apoptosis. Cell Death Differ 2007;14:1275–1284. CrossRef Google scholar

[8]	Rezaei-Ghaleh N, Amininasab M, Kumar S et al. Phosphorylation modifies the molecular stability of beta-amyloid deposits. Nat Commun 2016;7:11359. CrossRef Google scholar

[9]	Ries RJ, Zaccara S, Klein P et al. m(6)A enhances the phase separation potential of mRNA. Nature 2019;571:424–428. CrossRef Google scholar

[10]	Shi H, Zhang X, Weng YL et al. m(6)A facilitates hippocampus- dependent learning and memory through YTHDF1. Nature 2018;563:249–253. CrossRef Google scholar

[11]	Wang X, Lu Z, Gomez A et al. N6-methyladenosinedependent regulation of messenger RNA stability. Nature 2014;505:117–120. CrossRef Google scholar

[12]	Westermann B. Mitochondrial fusion and fission in cell life and death. Nat Rev Mol Cell Biol 2010;11:872–884. CrossRef Google scholar

[13]	Youmans KL, Leung S, Zhang J et al. Amyloid-beta42 alters apolipoprotein E solubility in brains of mice with five familial AD mutations. J Neurosci Methods 2011;196:51–59. CrossRef Google scholar

[14]	Zaccara S, Jaffrey SR. A unified model for the function of YTHDF proteins in regulating m(6)A-modified mRNA. Cell 2020;181:1582–1595.e18 e1518. CrossRef Google scholar

[15]	Zhao BS, Wang X, Beadell AV et al. m(6)A-dependent maternal mRNA clearance facilitates zebrafish maternal-to-zygotic transition. Nature 2017;542:475–478. CrossRef Google scholar