|
|
|
|
|
|
|
|
|||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
First published online 8 November 2005
doi: 10.1242/jcs.02669
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Research Article |
Laboratoire de Chimie Biologique, Institut de Biologie et de Médecine Moléculaires, Université Libre de Bruxelles, 6041 Gosselies, Belgium
Author for correspondence (e-mail: vkruys{at}ulb.ac.be)
Accepted 23 August 2005
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.
Key words: RNA-binding protein, Nuclear import, Nuclear export
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati 
Twitter What's this?
Related articles in JCS:
This article has been cited by other articles:
|
|
 |
|
  S. Souquere, S. Mollet, M. Kress, F. Dautry, G. Pierron, and D. Weil Unravelling the ultrastructure of stress granules and associated P-bodies in human cells J. Cell Sci., October 15, 2009; 122(20): 3619 - 3626. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Ernoult-Lange, A. Wilczynska, M. Harper, C. Aigueperse, F. Dautry, M. Kress, and D. Weil Nucleocytoplasmic Traffic of CPEB1 and Accumulation in Crm1 Nucleolar Bodies Mol. Biol. Cell, January 1, 2009; 20(1): 176 - 187. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Khacho, K. Mekhail, K. Pilon-Larose, A. Pause, J. Cote, and S. Lee eEF1A Is a Novel Component of the Mammalian Nuclear Protein Export Machinery Mol. Biol. Cell, December 1, 2008; 19(12): 5296 - 5308. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. M. Emara, H. Liu, W. G. Davis, and M. A. Brinton Mutation of Mapped TIA-1/TIAR Binding Sites in the 3' Terminal Stem-Loop of West Nile Virus Minus-Strand RNA in an Infectious Clone Negatively Affects Genomic RNA Amplification J. Virol., November 1, 2008; 82(21): 10657 - 10670. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Pullmann Jr., H. H. Kim, K. Abdelmohsen, A. Lal, J. L. Martindale, X. Yang, and M. Gorospe Analysis of Turnover and Translation Regulatory RNA-Binding Protein Expression through Binding to Cognate mRNAs Mol. Cell. Biol., September 15, 2007; 27(18): 6265 - 6278. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. McAlinden, L. Liang, Y. Mukudai, T. Imamura, and L. J. Sandell Nuclear Protein TIA-1 Regulates COL2A1 Alternative Splicing and Interacts with Precursor mRNA and Genomic DNA J. Biol. Chem., August 17, 2007; 282(33): 24444 - 24454. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. M. Izquierdo and J. Valcarcel Fas-activated Serine/Threonine Kinase (FAST K) Synergizes with TIA-1/TIAR Proteins to Regulate Fas Alternative Splicing J. Biol. Chem., January 19, 2007; 282(3): 1539 - 1543. [Abstract] [Full Text] [PDF]
|
|
