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

Autor:	Daria Sobańska, Alicja A Komur, Agnieszka Chabowska-Kita, Julita Gumna, Pooja Kumari, Katarzyna Pachulska-Wieczorek, Rafal Ciosk
Rok vydání:	2022
Předmět:	Ribonucleases Gene Expression Regulation Endoribonucleases Genetics Animals RNA-Binding Proteins RNA Messenger Caenorhabditis elegans
Zdroj:	Nucleic Acids Research. 50:8226-8239
ISSN:	1362-4962 0305-1048
DOI:	10.1093/nar/gkac609
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd55e0e88509a05ac7b472945a95839b https://doi.org/10.1093/nar/gkac609 Zobrazit plný text záznamu