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) 48 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 MTAuthor
Mark T. McNally PhD Associate Professor in the Microbiology and Immunology department at Medical College of WisconsinMESH 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
