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

Naoyuki Kataoka1, Michael D Diem, Mayumi Yoshida

  • 1Medical Top Track Program, Medical Research Institute, Tokyo Dental and Medical University, Tokyo 113-8510, Japan. kataoka.naoyuki.6m@kyoto-u.ac.jp

Scientific Reports
|February 23, 2012
PubMed

Insights

Researchers identified a Y14 nuclear localization signal (YNS) involved in mRNA export. This signal also mediates Magoh binding and mRNA association, revealing Y14

Area of Science:

  • Molecular Biology
  • Cell Biology
  • RNA Biology

Background:

  • Exon junction complexes (EJCs) are deposited on mRNAs during splicing.
  • The EJC core includes proteins like Y14 and Magoh, crucial for mRNA processing.
  • Y14 shuttles between the nucleus and cytoplasm and binds Magoh.

Purpose of the Study:

  • To delineate the Y14 nuclear localization signal (YNS) and its dual role in nuclear import and export.
  • To identify the region of Y14 responsible for Magoh binding and association with spliced mRNAs.
  • To investigate the functional significance of Y14 independent of Magoh.

Main Methods:

  • Site-directed mutagenesis to create Y14 mutants.
  • Nuclear localization and export assays.
  • Co-immunoprecipitation to assess protein-protein interactions.

Main Results:

  • A novel Y14 nuclear localization signal (YNS) was identified, mediating both nuclear import and export.
  • A 12-amino-acid peptide at the Y14 carboxyl terminus is essential for Magoh binding and mRNA association.
  • Y14 mutants lacking Magoh binding capability still localize to the nucleus.

Conclusions:

  • Y14 possesses a distinct nuclear localization signal (YNS) that regulates its nucleocytoplasmic shuttling.
  • Specific regions of Y14 are critical for its interaction with Magoh and recruitment to spliced mRNAs.
  • Y14 may have functions independent of Magoh, involving nuclear import pathways.

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