Publications by authors named "Aleksandra Sergeeva"
Cytosolic aggregation of the RNA binding protein TDP-43 (transactive response DNA-binding protein 43) is a hallmark of amyotrophic lateral sclerosis and frontotemporal dementia. Here, we report that during oxidative stress, TDP-43 becomes SUMO2/3-ylated by the SUMO E3 ligase protein PIAS4 (protein inhibitor of activated STAT 4) and enriches in cytoplasmic stress granules (SGs). Upon pharmacological inhibition of TDP-43 SUMO2/3-ylation or PIAS4 depletion, TDP-43 enrichment in SGs is accompanied by irreversible aggregation.
View Article and Find Full Text PDFCytosolic aggregation of the nuclear protein TDP-43 is associated with many neurodegenerative diseases, but the triggers for TDP-43 aggregation are still debated. Here, we demonstrate that TDP-43 aggregation requires a double event. One is up-concentration in stress granules beyond a threshold, and the other is oxidative stress.
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- Prions are unique proteins that can exist in different states, some of which can be passed down through generations, specifically in yeast proteins like Sup35 and Rnq1.
- Studies indicate that these prion states form aggregates that may have amyloid characteristics, but prior evidence in living organisms was lacking.
- The research successfully extracted native fibrils from yeast proteins, demonstrated their amyloid properties using Congo Red dye, and showed the potential to identify new amyloids across various organisms.
Article Synopsis
- Amyloids are responsible for incurable diseases in humans and animals, but they also play crucial roles in regulating important processes in bacteria and eukaryotes due to their unique properties like strength and elasticity.
- The review suggests a need for clear criteria to differentiate between well-proven functional amyloids and those showing only some amyloid characteristics, emphasizing the importance of demonstrating a cross-β structure in vivo.
- Current research highlights that functional amyloids should be searched for among structural and protective proteins, and new proteomic methods are paving the way for the systematic identification of these amyloids in various organisms.
The search for novel pathological and functional amyloids represents one of the most important tasks of contemporary biomedicine. Formation of pathological amyloid fibrils in the aging brain causes incurable neurodegenerative disorders such as Alzheimer's, Parkinson's Huntington's diseases. At the same time, a set of amyloids regulates vital processes in archaea, prokaryotes and eukaryotes.
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