Modulation of p53 and prion protein aggregation by RNA.

Authors:
Yraima Cordeiro
Yraima Cordeiro
Centro Nacional de Ressonância Magnética Nuclear Jiri Jonas
Brazil
Suparna Sanyal
Suparna Sanyal
Uppsala University
Sweden
Jerson L Silva
Jerson L Silva
Centro Nacional de Ressonância Magnética Nuclear Jiri Jonas
Brazil

Biochim Biophys Acta Proteins Proteom 2019 Feb 28. Epub 2019 Feb 28.

Instituto de Bioquímica Médica Leopoldo de Meis, Instituto Nacional de Ciência Tecnologia de Biologia Estrutural e Bioimagem, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil. Electronic address:

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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Source
http://dx.doi.org/10.1016/j.bbapap.2019.02.006DOI Listing
February 2019

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