HNS, a nuclear-cytoplasmic shuttling sequence in HuR
| Autor: | Joan A. Steitz, Xinhao Cynthia Fan |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Cytoplasm
Xenopus Molecular Sequence Data RNA-binding protein Biology Transfection Heterogeneous ribonucleoprotein particle ELAV-Like Protein 1 Heterogeneous-Nuclear Ribonucleoprotein K Mice Animals Humans Amino Acid Sequence RNA Messenger Nuclear protein Nuclear export signal Conserved Sequence Cell Nucleus Multidisciplinary Sequence Homology Amino Acid RNA-Binding Proteins 3T3 Cells Biological Sciences Molecular biology Recombinant Proteins Cell biology ELAV Proteins Ribonucleoproteins Antigens Surface Heterogeneous Nuclear Ribonucleoprotein A1 Nuclear transport Sequence Alignment Nuclear localization sequence HeLa Cells |
| Zdroj: | Proceedings of the National Academy of Sciences. 95:15293-15298 |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | Proteins are transported into and out of the cell nucleus via specific signals. The two best-studied nuclear transport processes are mediated either by classical nuclear localization signals or nuclear export signals. There also are shuttling sequences that direct the bidirectional transport of RNA-binding proteins. Two examples are the M9 sequence in heterogeneous nuclear ribonucleoprotein A1 and the heterogeneous nuclear ribonucleoprotein K shuttling domain (KNS) sequence in heterogeneous nuclear ribonucleoprotein K, both of which appear to contribute importantly to the export of mRNA to the cytoplasm. HuR is an RNA-binding protein that can stabilize labile mRNAs containing AU-rich elements in their 3′ untranslated regions and has been shown to shuttle between the nucleus and cytoplasm (18, 19). We have identified in HuR a shuttling sequence that also possess transcription-dependent nuclear localization signal activity. We propose that HuR first may bind AU-rich element-containing mRNAs in the nucleus and then escort them through the nuclear pore, providing protection during and after export to the cytoplasmic compartment. |
| Databáze: | OpenAIRE |
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