Modulation of p53 and prion protein aggregation by RNA |
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| Affiliation: | 1. Faculty of Pharmacy, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil;2. 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;3. Department of Cell and Molecular Biology, Uppsala University, Uppsala, Box-596, 75124, Sweden;1. Physical Chemistry Division, CSIR-National Chemical Laboratory, Pune 411008, India;2. Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India;3. Department of Biological Sciences, Indian Institute of Science Education and Research Kolkata, Mohanpur 741246, India;4. Centre for Advanced Functional Materials (CAFM), Indian Institute of Science Education and Research Kolkata, Mohanpur 741246, India |
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| 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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