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Mol Cell Biol ; 30(10): 2552-62, 2010 May.
Article in English | MEDLINE | ID: mdl-20308327

ABSTRACT

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.


Subject(s)
Active Transport, Cell Nucleus/physiology , Glycine/metabolism , Heterogeneous-Nuclear Ribonucleoprotein Group F-H , beta Karyopherins/metabolism , Alternative Splicing , Amino Acid Sequence , Cell Nucleus/chemistry , Cell Nucleus/metabolism , HeLa Cells , Heterogeneous-Nuclear Ribonucleoprotein Group F-H/genetics , Heterogeneous-Nuclear Ribonucleoprotein Group F-H/metabolism , Humans , Molecular Sequence Data , Mutation , Nuclear Localization Signals/metabolism , Protein Processing, Post-Translational , Protein Structure, Tertiary , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Sequence Alignment , beta Karyopherins/genetics
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