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SHR Neuro Krebs Kardio Lipid Stoffw Microb

Lenard, AJ; Zhou, Q; Madreiter-Sokolowski, C; Bourgeois, B; Habacher, H; Khanna, Y; Madl, T.
EGCG Promotes FUS Condensate Formation in a Methylation-Dependent Manner.
Cells. 2022; 11(4): Doi: 10.3390/cells11040592 [OPEN ACCESS]
Web of Science PubMed PUBMED Central FullText FullText_MUG


Führende Autor*innen der Med Uni Graz
Lenard Aneta
Madl Tobias
Zhou Qishun
Co-Autor*innen der Med Uni Graz
Bourgeois Benjamin Michel Rene
Habacher Hermann Hans
Khanna Yukti
Madreiter-Sokolowski Corina

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Millions of people worldwide are affected by neurodegenerative diseases (NDs), and to date, no effective treatment has been reported. The hallmark of these diseases is the formation of pathological aggregates and fibrils in neural cells. Many studies have reported that catechins, polyphenolic compounds found in a variety of plants, can directly interact with amyloidogenic proteins, prevent the formation of toxic aggregates, and in turn play neuroprotective roles. Besides harboring amyloidogenic domains, several proteins involved in NDs possess arginine-glycine/arginine-glycine-glycine (RG/RGG) regions that contribute to the formation of protein condensates. Here, we aimed to assess whether epigallocatechin gallate (EGCG) can play a role in neuroprotection via direct interaction with such RG/RGG regions. We show that EGCG directly binds to the RG/RGG region of fused in sarcoma (FUS) and that arginine methylation enhances this interaction. Unexpectedly, we found that low micromolar amounts of EGCG were sufficient to restore RNA-dependent condensate formation of methylated FUS, whereas, in the absence of EGCG, no phase separation could be observed. Our data provide new mechanistic roles of EGCG in the regulation of phase separation of RG/RGG-containing proteins, which will promote understanding of the intricate function of EGCG in cells.

Find related publications in this database (Keywords)
neurodegenerative diseases
arginine methylation
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