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Molecular and Cellular Biology, October 2003, p. 6780-6789, Vol. 23, No. 19
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.19.6780-6789.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Targeted Disruption of the Mouse PAS Domain Serine/Threonine Kinase PASKIN

Dörthe M. Katschinski,1 Hugo H. Marti,2 Klaus F. Wagner,3,4 Junpei Shibata,3,4 Katrin Eckhardt,5 Falk Martin,5 Reinhard Depping,3 Uwe Paasch,6 Max Gassmann,7 Birgit Ledermann,8 Isabelle Desbaillets,7,{dagger} and Roland H. Wenger5*

Cell Physiology Group, Medical Faculty, Martin Luther University Halle, D-06112 Halle,1 Institute of Physiology,3 Clinic of Anaesthesiology, University of Lübeck, D-23538 Lübeck,4 Carl Ludwig Institute of Physiology,5 Clinic of Dermatology University of Leipzig, D-04103 Leipzig, Germany,6 Institutes of Physiology,2 Veterinary Physiology,7 Laboratory Animal Science, University of Zürich, CH-8057 Zürich, Switzerland8

Received 31 March 2003/ Returned for modification 28 May 2003/ Accepted 30 June 2003

PASKIN is a novel mammalian serine/threonine kinase containing two PAS (Per-Arnt-Sim) domains. PASKIN is related to the Rhizobium oxygen sensor protein FixL and to AMP-regulated kinases. Like FixL, the sensory PAS domain of PASKIN controls the kinase activity by autophosphorylation in a (unknown) ligand-dependent manner. In Saccharomyces cerevisiae, the two PASKIN orthologues PSK1 and PSK2 phosphorylate three translation factors and two enzymes involved in glycogen synthesis, thereby coordinately regulating protein synthesis and glycolytic flux. To elucidate the function of mammalian PASKIN, we inactivated the mouse Paskin gene by homologous recombination in embryonic stem cells. Paskin-/- mice showed normal development, growth, and reproduction. The targeted integration of a lacZ reporter gene allowed the identification of the cell types expressing mouse PASKIN. Surprisingly, PASKIN expression is strongly upregulated in postmeiotic germ cells during spermatogenesis. However, fertility and sperm production and motility were not affected by the PASKIN knockout. The Ppp1r7 gene encoding Sds22, a regulatory subunit of protein phosphatase 1, shares the promoter region with the Paskin gene, pointing towards a common transcriptional regulation. Indeed, Sds22 colocalized with the cell types expressing PASKIN in vivo, suggesting a functional role of protein phosphatase-1 in the regulation of PASKIN autophosphorylation.

* Corresponding author. Mailing address: Carl Ludwig Institute of Physiology, University of Leipzig, Liebigstrasse 27, D-04103 Leipzig, Germany. Phone: 49 0 341 97 15567. Fax: 49 0 341 97 15509. E-mail: wenr{at}medizin.uni-leipzig.de.

{dagger} Present address: Laboratory of Tumor Biology and Genetics, Centre Hospitalier Universitaire Vaudois, CH-1011 Lausanne, Switzerland.

Molecular and Cellular Biology, October 2003, p. 6780-6789, Vol. 23, No. 19
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.19.6780-6789.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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