Literature DB >> 12773480

The dsRNA binding protein family: critical roles, diverse cellular functions.

Laura R Saunders1, Glen N Barber.   

Abstract

The dsRNA binding proteins (DRBPs) comprise a growing family of eukaryotic, prokaryotic, and viral-encoded products that share a common evolutionarily conserved motif specifically facilitating interaction with dsRNA. Proteins harboring dsRNA binding domains (DRBDs) have been reported to interact with as little as 11 bp of dsRNA, an event that is independent of nucleotide sequence arrangement. More than 20 DRBPs have been identified and reportedly function in a diverse range of critically important roles in the cell. Examples include the dsRNA-dependent protein kinase PKR that functions in dsRNA signaling and host defense against virus infection and DICER, which is implicated in RNA interference (RNAi) -mediated gene silencing. Other DRBPs such as Staufen, adenosine deaminase acting on RNA (ADAR), and spermatid perinuclear RNA binding protein (SPNR) are known to play essential roles in development, translation, RNA editing, and stability. In many cases, homozygous and even heterozygous disruption of DRBPs in animal models results in embryonic lethality. These results implicate the recognition of dsRNA as an evolutionarily conserved mechanism important in the regulation of gene expression and in host defense and underscore the diversity of essential biological tasks performed by dsRNA-related processes in the cell.

Entities:  

Mesh:

Substances:

Year:  2003        PMID: 12773480     DOI: 10.1096/fj.02-0958rev

Source DB:  PubMed          Journal:  FASEB J        ISSN: 0892-6638            Impact factor:   5.191


  145 in total

1.  Xenopus staufen2 is required for anterior endodermal organ formation.

Authors:  Cassandra K Bilogan; Marko E Horb
Journal:  Genesis       Date:  2012-02-17       Impact factor: 2.487

2.  Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III.

Authors:  Haihong Wu; Anthony Henras; Guillaume Chanfreau; Juli Feigon
Journal:  Proc Natl Acad Sci U S A       Date:  2004-05-18       Impact factor: 11.205

3.  Characterization of Staufen 1 ribonucleoprotein complexes.

Authors:  Cornelia Brendel; Monika Rehbein; Hans-Jürgen Kreienkamp; Friedrich Buck; Dietmar Richter; Stefan Kindler
Journal:  Biochem J       Date:  2004-12-01       Impact factor: 3.857

4.  Detection of genome-scale ordered RNA structure (GORS) in genomes of positive-stranded RNA viruses: Implications for virus evolution and host persistence.

Authors:  Peter Simmonds; Andrew Tuplin; David J Evans
Journal:  RNA       Date:  2004-07-23       Impact factor: 4.942

Review 5.  Induction of RNA interference in dendritic cells.

Authors:  Mu Li; Hua Qian; Thomas E Ichim; Wei-Wen Ge; Igor A Popov; Katarzyna Rycerz; John Neu; David White; Robert Zhong; Wei-Ping Min
Journal:  Immunol Res       Date:  2004       Impact factor: 2.829

6.  Evidence for a cytoplasmic microprocessor of pri-miRNAs.

Authors:  Jillian S Shapiro; Ryan A Langlois; Alissa M Pham; Benjamin R Tenoever
Journal:  RNA       Date:  2012-05-25       Impact factor: 4.942

7.  High affinity, dsRNA binding by disconnected interacting protein 1.

Authors:  Daniel J Catanese; Kathleen S Matthews
Journal:  Biochem Biophys Res Commun       Date:  2010-07-17       Impact factor: 3.575

8.  Dynamic origins of differential RNA binding function in two dsRBDs from the miRNA "microprocessor" complex.

Authors:  Christopher Wostenberg; Kaycee A Quarles; Scott A Showalter
Journal:  Biochemistry       Date:  2010-11-22       Impact factor: 3.162

9.  Structural insights reveal the specific recognition of roX RNA by the dsRNA-binding domains of the RNA helicase MLE and its indispensable role in dosage compensation in Drosophila.

Authors:  Mengqi Lv; Yixiang Yao; Fudong Li; Ling Xu; Lingna Yang; Qingguo Gong; Yong-Zhen Xu; Yunyu Shi; Yu-Jie Fan; Yajun Tang
Journal:  Nucleic Acids Res       Date:  2019-04-08       Impact factor: 16.971

10.  Disruption of the NHR4 domain structure in AML1-ETO abrogates SON binding and promotes leukemogenesis.

Authors:  Eun-Young Ahn; Ming Yan; Oxana A Malakhova; Miao-Chia Lo; Anita Boyapati; Hans Beier Ommen; Robert Hines; Peter Hokland; Dong-Er Zhang
Journal:  Proc Natl Acad Sci U S A       Date:  2008-10-24       Impact factor: 11.205

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.