Identification of the sequence determinants mediating the nucleo-cytoplasmic shuttling of TIAR and TIA-1 RNA-binding proteins
Autor: | Georges Huez, Nathalie Delestienne, Tong Zhang, Véronique Kruys, Cyril Gueydan |
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Rok vydání: | 2005 |
Předmět: |
Cytoplasm
Transcription Genetic -- genetics Cell Nucleus -- metabolism Transcription Genetic Nuclear export Nuclear import RNA-binding protein Amino Acid Motifs Molecular Sequence Data Active Transport Cell Nucleus RNA Polymerase II -- metabolism Biology Cercopithecus aethiops Mice Chlorocebus aethiops Animals cardiovascular diseases Amino Acid Sequence Nuclear export signal RNA-Binding Proteins -- genetics Cell Nucleus RNA RNA-Binding Proteins Cell Biology Amino Acid Motifs -- physiology Sciences bio-médicales et agricoles Subcellular localization Cytoplasm -- genetics RNA-Binding Proteins -- metabolism Molecular biology Cell biology nervous system diseases Active Transport Cell Nucleus -- physiology RNA Polymerase II -- genetics T-Cell Intracellular Antigen-1 Transcription Genetic -- physiology Cytoplasm -- metabolism Cell Nucleus -- genetics RNA splicing COS Cells RNA Polymerase II Nuclear transport Precursor mRNA |
Zdroj: | Journal of cell science, 118 (Pt 23 |
ISSN: | 0021-9533 |
Popis: | TIAR and TIA-1 are two closely related RNA-binding proteins which possess three RNA recognition motifs (RRMs) followed by an auxiliary region. These proteins are involved in several mechanisms of RNA metabolism, including alternative hnRNA splicing and regulation of mRNA translation. Here we characterize the subcellular localization of these proteins in somatic cells. We demonstrate that TIAR and TIA-1 continuously shuttle between the cytoplasm and the nucleus and belong to the class of RNA-binding proteins whose nuclear import is transcription-dependent. We identified RRM2 and the first half of the auxiliary region as important determinants for TIAR and TIA-1 nuclear accumulation. In contrast, the nuclear export of TIAR and TIA-1 is mediated by RRM3. Both RRMs contribute to TIAR and TIA-1 nuclear accumulation or export by their RNA-binding capacity. Indeed, whereas mutations of the highly conserved RNP2 or RNP1 peptides in RRM2 redistribute TIAR to the cytoplasm, similar modifications in RRM3 abolish TIAR nuclear export. Moreover, TIAR and TIA-1 nuclear accumulation is a Ran-GTP-dependent pathway, in contrast to its nuclear export which is unaffected by Ran-GTP depletion and which is independent of the major CRM1-exporting pathway. This study demonstrates the importance of TIAR and TIA-1 RNA-binding domains for their subcellular localization and provides the first evidence for distinct functions of TIAR and TIA-1 RRMs. Journal Article Research Support, Non-U.S. Gov't SCOPUS: ar.j info:eu-repo/semantics/published |
Databáze: | OpenAIRE |
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