Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-1283
Katschinski, D M; Marti, H H; Wagner, K F; Shibata, J; Eckhardt, K; Martin, F; Depping, R; Paasch, U; Gassmann, M; Ledermann, B; Desbaillets, I; Wenger, R H (2003). Targeted disruption of the mouse PAS domain serine/threonine kinase PASKIN. Molecular and Cellular Biology, 23(19):6780-6789.
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.
|Item Type:||Journal Article, refereed|
|Communities & Collections:||04 Faculty of Medicine > Institute of Physiology
07 Faculty of Science > Institute of Physiology
|DDC:||570 Life sciences; biology|
|Deposited On:||11 Feb 2008 12:22|
|Last Modified:||27 Nov 2013 19:29|
|Publisher:||American Society for Microbiology (ASM)|
|Additional Information:||Copyright © 2007, the American Society for Microbiology. All rights reserved|
|Citations:||Web of Science®. Times Cited: 21|
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