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Originally published In Press as doi:10.1074/jbc.M104755200 on August 16, 2001

J. Biol. Chem., Vol. 276, Issue 43, 40175-40182, October 26, 2001
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Cloning and Characterization of an Alternatively Spliced Form of SR Protein Kinase 1 That Interacts Specifically with Scaffold Attachment Factor-B*

Eleni NikolakakiDagger §, Rachel Kohen, Annette M. Hartmann||, Stefan Stamm**, Elena Georgatsou, and Thomas GiannakourosDagger

From the Dagger  Laboratory of Biochemistry, School of Chemistry, The Aristotelian University of Thessaloniki, Thessaloniki 54006, Greece, the  Laboratory of Biochemistry, Medical School, University of Thessaly, Larissa 41222, Greece, the || Ludwig Maximilian University, Nussbaumstrasse 7, München 80336, Germany, and the ** Institute of Biochemistry, University of Erlangen-Nurenberg, Fahrstrasse 17, Erlangen 91054, Germany

Serine/arginine protein kinases have been conserved throughout evolution and are thought to play important roles in the regulation of mRNA processing, nuclear import, germline development, polyamine transport, and ion homeostasis. Human SRPK1, which was first identified as a kinase specific for the SR family of splicing factors, is located on chromosome 6p21.2-p21.3. We report here the cloning and characterization of SRPK1a, which is encoded by an alternatively processed transcript derived from the SRPK1 gene. SRPK1a contains an insertion of 171 amino acids at its NH2-terminal domain and is similar to SRPK1 in substrate specificity and subcellular localization. Moreover, both isoforms can induce alternative splicing of human tau exon 10 in transfected cells. Using the yeast two-hybrid assay, we found that the extended NH2-terminal domain of SRPK1a interacts with Scaffold Attachment Factor-B, a nuclear scaffold-associated protein. Confirmation of this interaction was provided by in vitro binding assays, as well as by co-immunoprecipitation from 293T cells doubly transfected with SRPK1a and SAF-B. Our studies suggest that different SRPK family members are uniquely regulated and targeted and thus the multiple SRPK kinases present in higher eukaryotes may perform specialized and differentiable functions.

* This work was supported by grants from the Greek Secretariat of Research and Technology (Pi ENEDelta 1999 to T. G. and E. G.), from the Greek Ministry of Education (Pi .Sigma .E to E. G.), and from the Deutsche Forschungsgemeinschaft (SFB 473) and the Johannes and Frieda Marohn Stiftung (to S. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ318054 and AJ224115.

§ To whom correspondence should be addressed: Laboratory of Biochemistry, School of Chemistry, Aristotelian University of Thessaloniki, Thessaloniki 54006, Greece. Tel.: 30-31-997726; Fax: 30-31-997689; E-mail: nikol@ccf.auth.gr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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