Specific Y14 domains mediate its nucleo-cytoplasmic shuttling and association with spliced mRNA.

Scientific Reports
Naoyuki KataokaMutsuhito Ohno

Abstract

Pre-mRNA splicing deposits multi-protein complexes, termed exon junction complexes (EJCs), on mRNAs near exon-exon junctions. The core of EJC consists of four proteins, eIF4AIII, MLN51, Y14 and Magoh. Y14 is a nuclear protein that can shuttle between the nucleus and the cytoplasm, and binds specifically to Magoh. Here we delineate a Y14 nuclear localization signal that also confers its nuclear export, which we name YNS. We further identified a 12-amino-acid peptide near Y14's carboxyl terminus that is required for its association with spliced mRNAs, as well as for Magoh binding. Furthermore, the Y14 mutants, which are deficient in binding to Magoh, could still be localized to the nucleus, suggesting the existence of both the nuclear import pathway and function for Y14 unaccompanied by Magoh.

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Citations

Aug 21, 2013·Histochemistry and Cell Biology·Yasuhito IshigakiNaohisa Tomosugi
Feb 12, 2015·International Journal of Molecular Sciences·So MasakiNaoyuki Kataoka
Apr 14, 2015·Biomolecules·Tzu-Wei ChuangWoan-Yuh Tarn
Feb 22, 2017·Scientific Reports·Jo-Hsi HuangChia-Ying Chu
Jan 14, 2018·Scientific Reports·Takanori Tatsuno, Yasuhito Ishigaki
Feb 13, 2020·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·So MasakiNaoyuki Kataoka

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Methods Mentioned

BETA
immunoprecipitation
PCRs
PCR
transfection
in vitro transcription

Software Mentioned

Magoh

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