About: Dissecting the roles of TRBP and PACT in double‐stranded RNA recognition and processing of noncoding RNAs

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About: Dissecting the roles of TRBP and PACT in double‐stranded RNA recognition and processing of noncoding RNAs Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Dissecting the roles of TRBP and PACT in double‐stranded RNA recognition and processing of noncoding RNAs
Creator	Heyam, Alex Lagos, Dimitris Plevin, Michael
source	Medline; PMC
abstract	HIV TAR RNA‐binding protein (TRBP) and Protein Activator of PKR (PACT) are double‐stranded (ds) RNA‐binding proteins that participate in both small regulatory RNA biogenesis and the response to viral dsRNA. Despite considerable progress toward understanding the structure–function relationship of TRBP and PACT, their specific roles in these seemingly distinct cellular pathways remain unclear. Both proteins are composed of three copies of the double‐stranded RNA‐binding domain, two of which interact with dsRNA, while the C‐terminal copy mediates protein–protein interactions. PACT and TRBP are found in a complex with the endonuclease Dicer and facilitate processing of immature microRNAs. Their precise contribution to the Dicing step has not yet been defined: possibilities include precursor recruitment, rearrangement of dsRNA within the complex, loading the processed microRNA into the RNA‐induced silencing complex, and distinguishing different classes of small dsRNA. TRBP and PACT also interact with the viral dsRNA sensors retinoic acid‐inducible gene I (RIG‐I) and double‐stranded RNA‐activated protein kinase (PKR). Current models suggest that PACT enables RIG‐I to detect a wider range of viral dsRNAs, while TRBP and PACT exert opposing regulatory effects on PKR. Here, the evidence that implicates TRBP and PACT in regulatory RNA processing and viral dsRNA sensing is reviewed and discussed in the context of their molecular structure. The broader implications of a link between microRNA biogenesis and the innate antiviral response pathway are also considered. WIREs RNA 2015, 6:271–289. doi: 10.1002/wrna.1272 1.. RNA Interactions with Proteins and Other Molecules > Protein–RNA Interactions: Functional Implications; 2.. RNA Turnover and Surveillance > Turnover/Surveillance Mechanisms; 3.. Regulatory RNAs/RNAi/Riboswitches > Biogenesis of Effector Small RNAs.
has issue date	2015-01-28(xsd:dateTime)
bibo:doi	10.1002/wrna.1272
bibo:pmid	25630541
has license	no-cc
sha1sum (hex)	d6563aa5b6e860e5f4679df0aa453215391295e5
schema:url	https://doi.org/10.1002/wrna.1272
resource representing a document's title	Dissecting the roles of TRBP and PACT in double‐stranded RNA recognition and processing of noncoding RNAs
has PubMed Central identifier	PMC7169789
has PubMed identifier	25630541
schema:publication	Wiley Interdiscip Rev RNA
resource representing a document's body	covid:d6563aa5b6e860e5f4679df0aa453215391295e5#body_text
is schema:about of	named entity 'RNA' named entity 'PKR' named entity 'proteins' named entity 'RNA-induced silencing complex' named entity 'cellular' named entity 'viral' named entity 'noncoding' named entity 'RECRUITMENT' named entity 'CONTEXT' named entity 'CONTRIBUTION' named entity 'DOUBLE-STRANDED RNA-BINDING DOMAIN' named entity 'CLASSES' named entity 'SUGGEST' named entity 'MICRORNA BIOGENESIS' named entity 'CONSIDERED' named entity 'HIV' named entity 'REGULATORY RNA' named entity 'BINDING PROTEIN' named entity 'EVIDENCE' named entity 'REVIEWED' named entity 'opposing' named entity 'range' named entity 'copy' named entity 'RIG-I' named entity 'C-terminal' named entity 'interact' named entity 'possibilities' named entity 'effects' named entity 'microRNAs' named entity 'dsRNA' named entity 'processing' named entity 'complex' named entity 'domain' named entity 'RNA' named entity 'PKR' named entity 'RIG-I' named entity 'RNA-binding proteins' named entity 'retinoic acid' named entity 'TRBP' named entity 'dsRNA' named entity 'protein-protein interactions' named entity 'dsRNA' named entity 'dsRNA' named entity 'Dicer' named entity 'microRNA' named entity 'biogenesis' named entity 'binding domain' named entity 'antiviral' named entity 'RNA processing' named entity 'interact' named entity 'HIV' named entity 'RNA-binding protein' named entity 'double-stranded' named entity 'Protein' named entity 'molecular structure' named entity 'TRBP' named entity 'double-stranded RNA-activated protein kinase' covid:arg/d6563aa5b6e860e5f4679df0aa453215391295e5 named entity 'wider' named entity 'loading' named entity 'microRNAs' named entity 'double-stranded RNA' named entity 'TRBP' named entity 'MEDIATES' named entity 'endonuclease' named entity 'RIG-I' named entity 'RNA-induced silencing complex' named entity 'interact' named entity 'inducible gene' named entity 'cellular pathways' named entity 'TRBP' named entity 'DISTINCT' named entity 'EFFECTS' named entity 'REARRANGEMENT' named entity 'ENABLES' named entity 'SMALL' named entity 'PROTEIN-PROTEIN INTERACTIONS' named entity 'STRUCTURE-FUNCTION RELATIONSHIP' named entity 'DOUBLE-STRANDED RNA'

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