دورية أكاديمية

The silencing of ets-4 mRNA relies on the functional cooperation between REGE-1/Regnase-1 and RLE-1/Roquin-1

التفاصيل البيبلوغرافية
العنوان: The silencing of ets-4 mRNA relies on the functional cooperation between REGE-1/Regnase-1 and RLE-1/Roquin-1
المؤلفون: Sobańska, Daria, Komur, Alicja A, Chabowska-Kita, Agnieszka, Gumna, Julita, Kumari, Pooja, Pachulska-Wieczorek, Katarzyna, Ciosk, Rafal
المساهمون: Research Council of Norway, National Science Centre, Poland, The European Molecular Biology Organization, Institute of Bioorganic Chemistry, Polish Academy of Sciences
المصدر: Nucleic Acids Research ; volume 50, issue 14, page 8226-8239 ; ISSN 0305-1048 1362-4962
بيانات النشر: Oxford University Press (OUP)
سنة النشر: 2022
مصطلحات موضوعية: Genetics
الوصف: Regnase-1 is an evolutionarily conserved endoribonuclease. It degrades diverse mRNAs important for many biological processes including immune homeostasis, development and cancer. There are two competing models of Regnase-1-mediated mRNA silencing. One model postulates that Regnase-1 works together with another RNA-binding protein, Roquin-1, which recruits Regnase-1 to specific mRNAs. The other model proposes that the two proteins function separately. Studying REGE-1, the Caenorhabditis elegans ortholog of Regnase-1, we have uncovered its functional relationship with RLE-1, the nematode counterpart of Roquin-1. While both proteins are essential for mRNA silencing, REGE-1 and RLE-1 appear to associate with target mRNA independently of each other. Thus, although the functional interdependence between REGE-1/Regnase-1 and RLE-1/Roquin-1 is conserved, the underlying mechanisms may display species-specific variation, providing a rare perspective on the evolution of this important post-transcriptional regulatory mechanism.
نوع الوثيقة: article in journal/newspaper
اللغة: English
DOI: 10.1093/nar/gkac609
الإتاحة: https://doi.org/10.1093/nar/gkac609Test
https://academic.oup.com/nar/article-pdf/50/14/8226/45289700/gkac609.pdfTest
حقوق: https://creativecommons.org/licenses/by/4.0Test/
رقم الانضمام: edsbas.38FFCB6E
قاعدة البيانات: BASE