INVESTIGADORES
BOCCACCIO Graciela Lidia
artículos
Título:
The double-stranded RNA binding protein Staufen: from embryo polarity to the stress response and neurodegeneration
Autor/es:
MARTINEZ TOSAR L J; THOMAS, MG; BAEZ, MV; IBAÑEZ; CHERNOMORETZ, ; BOCCACCIO, GL
Revista:
FRONTIERS IN BIOSCIENCE-LANDMARK
Editorial:
FRONTIERS IN BIOSCIENCE INC
Referencias:
Año: 2012 vol. 4 p. 432 - 452
ISSN:
1093-9946
Resumen:
Staufen is a
double-stranded RNA-binding protein that forms RNA granules by means of
RNA-dependent and -independent intermolecular interactions. Staufen was
initially described in Drosophila as a key molecule for
targeting maternal mRNAs in the developing embryo. In vertebrates, two highly
similar paralogs with several splicing variants mediate mRNA transport in
neurons, thus affecting plasticity, learning and memory. In addition, a role for
Staufen in translation activation and mRNA decay is apparent. In recent years,
Staufen was shown to be an important regulatory component of stress granules
(SGs), which are large aggregates of silenced mRNPs specifically induced upon
acute cellular stress. SGs contribute to cell survival by reprogramming
translation and inhibiting pro-apoptotic pathways and Staufen appears to
negatively modulate SG formation by several mechanisms. More recently,
mammalian Staufen was found in RNA granules and pathological cytoplasmic aggregates
related to SGs containing huntingtin, TDP43, FUS/TLS or FMRP. In addition, Staufen
binds CUG repeats present in mutant RNAs causative of degenerative conditions, thus
ameliorating disease. Finally, Staufen affects HIV and influenza infection at several
levels. Collectively, these observations unveil important roles for
Staufen-mediated posttranscriptional regulation in a growing number of human
diseases.