A glycine-rich domain of hnRNP H/F promotes nucleocytoplasmic shuttling and nuclear import through an interaction with transportin 1. Mol Cell Biol 2010 May;30(10):2552-62
Date
03/24/2010Pubmed ID
20308327Pubmed Central ID
PMC2863714DOI
10.1128/MCB.00230-09Scopus ID
2-s2.0-77951990307 (requires institutional sign-in at Scopus site) 55 CitationsAbstract
Heterogeneous nuclear ribonucleoprotein (hnRNP) H and F are members of a closely related subfamily of hnRNP proteins that are implicated in many aspects of RNA processing. hnRNP H and F are alternative splicing factors for numerous U2- and U12-dependent introns. The proteins have three RNA binding domains and two glycine-rich domains and localize to both the nucleus and cytoplasm, but little is known about which domains govern subcellular localization or splicing activity. We show here that the central glycine-tyrosine-arginine-rich (GYR) domain is responsible for nuclear localization, and a nonclassical nuclear localization signal (NLS) was mapped to a short, highly conserved sequence whose activity was compromised by point mutations. Glutathione S-transferase (GST) pulldown assays demonstrated that the hnRNP H NLS interacts with the import receptor transportin 1. Finally, we show that hnRNP H/F are transcription-dependent shuttling proteins. Collectively, the results suggest that hnRNP H and F are GYR domain-dependent shuttling proteins whose posttranslational modifications may alter nuclear localization and hence function.
Author List
Van Dusen CM, Yee L, McNally LM, McNally MTMESH terms used to index this publication - Major topics in bold
Active Transport, Cell NucleusAlternative Splicing
Amino Acid Sequence
Cell Nucleus
Glycine
HeLa Cells
Heterogeneous-Nuclear Ribonucleoprotein Group F-H
Humans
Molecular Sequence Data
Mutation
Nuclear Localization Signals
Protein Processing, Post-Translational
Protein Structure, Tertiary
Recombinant Fusion Proteins
Sequence Alignment
beta Karyopherins
