A brave new world of RNA-binding proteins

By Matthias W. Hentze, Alfredo Castello, T. Schwarzl, T. Preiss. Nature reviews. Molecular cell biology, 2018

1,521 citations recorded by the source corpus.

RNA-binding proteins (RBPs) are typically thought of as proteins that bind RNA through one or multiple globular RNA-binding domains (RBDs) and change the fate or function of the bound RNAs. Several hundred such RBPs have been discovered and investigated over the years. Recent proteome-wide studies have more than doubled the number of proteins implicated in RNA binding and uncovered hundreds of additional RBPs lacking conventional RBDs. In this Review, we discuss these new RBPs and the emerging understanding of their unexpected modes of RNA binding, which can be mediated by intrinsically disordered regions, protein–protein interaction interfaces and enzymatic cores, among others. We also discuss the RNA targets and molecular and cellular functions of the new RBPs, as well as the possibility that some RBPs may be regulated by RNA rather than regulate RNA.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/c176de3d5e2d942af3eb0f11f86b02911224371a

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Citations in the corpus

How RNA binding proteins interact with RNA: molecules and mechanisms (2020, background): “Found on opposite sides of the Argonaute protein, both domains facilitate binding of small interfering RNA and microRNA guides to mRNA targets (Höck and Meister, 2008).”
NRF2, a Transcription Factor for Stress Response and Beyond (2020, background): “In neuroblastoma cells, miR-153, miR-27a, miR142-5p, and miR-144 directly target 3′-untranslated region (UTR) of NFE2L2 and changes in these miRNAs either individually or as a group could result in inefficient transactivating ability of NRF2 [45].”
OpenCell: proteome-scale endogenous tagging enables the cartography of human cellular organization (2022, neutral): “Itwouldbefascinating toexploretheextenttowhichRNAitselfmight actasastructuralorganizerofthecellular proteome( 62 , 82 ).”