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4EHP-independent repression of endogenous mRNAs by the RNA-binding protein GIGYF2.

Abstract：

:Initially identified as a factor involved in tyrosine kinase receptor signaling, Grb10-interacting GYF protein 2 (GIGYF2) has later been shown to interact with the 5' cap-binding protein 4EHP as part of a translation repression complex, and to mediate post-transcriptional repression of tethered reporter mRNAs. A current model proposes that GIGYF2 is indirectly recruited to mRNAs by specific RNA-binding proteins (RBPs) leading to translation repression through its association with 4EHP. Accordingly, we recently observed that GIGYF2 also interacts with the miRNA-induced silencing complex and probably modulates its translation repression activity. Here we have further investigated how GIGYF2 represses mRNA function. In a tethering reporter assay, we identify three independent domains of GIGYF2 with repressive activity. In this assay, GIGYF2-mediated repression is independent of 4EHP but largely dependent on the CCR4/NOT complex that GIGYF2 recruits through multiple interfaces. Importantly, we show that GIGYF2 is an RBP and identify for the first time endogenous mRNA targets that recapitulate 4EHP-independent repression. Altogether, we propose that GIGYF2 has two distinct mechanisms of repression: one depends on 4EHP binding and mainly affects translation; the other is 4EHP-independent and involves the CCR4/NOT complex and its deadenylation activity.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Amaya Ramirez CC,Hubbe P,Mandel N,Béthune J

doi

10.1093/nar/gky198

subject

Has Abstract

pub_date

2018-06-20 00:00:00

pages

5792-5808

issue

11

eissn

0305-1048

issn

1362-4962

pii

4937549

journal_volume

46

pub_type

杂志文章

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