Nuclear export and retention signals in the RS domain of SR proteins

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

URL: http://www.ncbi.nlm.nih.gov/pubmed/12215544
DOI: 10.1128/MCB.22.19.6871-6882.2002

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
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: http://repository.cshl.edu/id/eprint/28685

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