Unknown

Dataset Information

0

Staufen-mediated mRNA decay.


ABSTRACT: Staufen1 (STAU1)-mediated mRNA decay (SMD) is an mRNA degradation process in mammalian cells that is mediated by the binding of STAU1 to a STAU1-binding site (SBS) within the 3'-untranslated region (3'-UTR) of target mRNAs. During SMD, STAU1, a double-stranded (ds) RNA-binding protein, recognizes dsRNA structures formed either by intramolecular base pairing of 3'-UTR sequences or by intermolecular base pairing of 3'-UTR sequences with a long-noncoding RNA (lncRNA) via partially complementary Alu elements. Recently, STAU2, a paralog of STAU1, has also been reported to mediate SMD. Both STAU1 and STAU2 interact directly with the ATP-dependent RNA helicase UPF1, a key SMD factor, enhancing its helicase activity to promote effective SMD. Moreover, STAU1 and STAU2 form homodimeric and heterodimeric interactions via domain-swapping. Because both SMD and the mechanistically related nonsense-mediated mRNA decay (NMD) employ UPF1; SMD and NMD are competitive pathways. Competition contributes to cellular differentiation processes, such as myogenesis and adipogenesis, placing SMD at the heart of various physiologically important mechanisms.

SUBMITTER: Park E 

PROVIDER: S-EPMC3711692 | biostudies-literature | 2013 Jul-Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Staufen-mediated mRNA decay.

Park Eonyoung E   Maquat Lynne E LE  

Wiley interdisciplinary reviews. RNA 20130516 4


Staufen1 (STAU1)-mediated mRNA decay (SMD) is an mRNA degradation process in mammalian cells that is mediated by the binding of STAU1 to a STAU1-binding site (SBS) within the 3'-untranslated region (3'-UTR) of target mRNAs. During SMD, STAU1, a double-stranded (ds) RNA-binding protein, recognizes dsRNA structures formed either by intramolecular base pairing of 3'-UTR sequences or by intermolecular base pairing of 3'-UTR sequences with a long-noncoding RNA (lncRNA) via partially complementary Alu  ...[more]

Similar Datasets

| S-EPMC5798355 | biostudies-literature
| S-EPMC6838198 | biostudies-literature
2017-03-21 | GSE85455 | GEO
2017-12-31 | GSE89588 | GEO
| MSV000080146 | MassIVE
| S-EPMC3947523 | biostudies-literature
| S-EPMC10332406 | biostudies-literature
| S-EPMC4126864 | biostudies-literature
| S-EPMC4648321 | biostudies-literature
| S-EPMC6360860 | biostudies-literature