Mar 4, 2019

Modulation of p53 and prion protein aggregation by RNA

Biochimica Et Biophysica Acta. Proteins and Proteomics
Yraima CordeiroJerson L Silva

Abstract

Several RNA-binding proteins undergo reversible liquid-liquid phase transitions, which, in pathological conditions, might evolve into transitions to solid-state phases, giving rise to amyloid structures. Amyloidogenic and prion-like proteins, such as the tumor suppressor protein p53 and the mammalian prion protein (PrP), bind RNAs specifically or nonspecifically, resulting in changes in their propensity to undergo aggregation. Mutant p53 aggregation seems to play a crucial role in cancer through loss of function, negative dominance and gain of function. PrP conversion modulated by RNA results in highly toxic aggregates. Here, we review data on the modulatory action of RNAs on the aggregation of both proteins.

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Mentioned in this Paper

Major Prion Protein
Mutant Proteins
TP53
Amyloid Proteins
Protein Aggregation, Pathological
Amyloid
Binding (Molecular Function)
Structure
Malignant Neoplasms
RNA-Binding Proteins

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