Cazalla, D., Zhu, J., Manche, L., Huber, E., Krainer, A. R., Caceres, J. F. (October 2002) Nuclear export and retention signals in the RS domain of SR proteins. Molecular and Cellular Biology, 22 (19). pp. 6871-6882. ISSN 0270-7306
Abstract
Splicing factors of the SR protein family share a modular structure consisting of one or two RNA recognition motifs (RRMs) and a C-terminal RS domain rich in arginine and serine residues. The RS domain, which is extensively phosphorylated, promotes protein-protein interactions and directs subcellular localization and—in certain situations—nucleocytoplasmic shuttling of individual SR proteins. We analyzed mutant versions of human SF2/ASF in which the natural RS repeats were replaced by RD or RE repeats and compared the splicing and subcellular localization properties of these proteins to those of SF2/ASF lacking the entire RS domain or possessing a minimal RS domain consisting of 10 consecutive RS dipeptides (RS10). In vitro splicing of a pre-mRNA that requires an RS domain could take place when the mutant RD, RE, or RS10 domain replaced the natural domain. The RS10 version of SF2/ASF shuttled between the nucleus and the cytoplasm in the same manner as the wild-type protein, suggesting that a tract of consecutive RS dipeptides, in conjunction with the RRMs of SF2/ASF, is necessary and sufficient to direct nucleocytoplasmic shuttling. However, the SR protein SC35 has two long stretches of RS repeats, yet it is not a shuttling protein. We demonstrate the presence of a dominant nuclear retention signal in the RS domain of SC35.
Item Type: | Paper |
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Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > splicing factor |
CSHL Authors: | |
Communities: | CSHL labs > Krainer lab |
Depositing User: | Matt Covey |
Date: | October 2002 |
Date Deposited: | 10 Dec 2013 15:14 |
Last Modified: | 10 Dec 2013 15:14 |
PMCID: | PMC134038 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/28685 |
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