Research Abstract


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

2011年9月14日 Scientific Reports 1 : 92 doi: 10.1038/srep00092


片岡 直行1,2,5*, Michael D. Diem3, 吉田 真由美1,4, 畑井 千裕2, 土橋 泉1, Gideon Dreyfuss3, 萩原 正敏5 & 大野 睦人2*

  1. 東京医科歯科大学 難治疾患研究所
  2. 京都大学ウイルス研究所
  3. ペンシルベニア大学医学系大学院(米国)
  4. 京都大学大学院生命科学研究科
  5. 京都大学大学院医学研究科
    *These authors contributed equally to this work.
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.