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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-19386

Schlaefli, P; Borter, E; Spielmann, P; Wenger, R H (2009). The PAS-domain kinase PASKIN: a new sensor in energy homeostasis. Cellular and Molecular Life Sciences, 66(5):876-883.

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Abstract

The PAS domain kinase PASKIN, also termed PAS kinase or PASK, is an evolutionarily conserved potential sensor kinase related to the heme-based oxygen sensors of nitrogen-fixing bacteria. In yeast, the two PASKIN homologs link energy flux and protein synthesis following specific stress conditions. In mammals, PASKIN may regulate glycogen synthesis and protein translation. Paskin knock-out mice do not show any phenotype under standard animal husbandry conditions. Interestingly, these mice seem to be protected from the symptoms of the metabolic syndrome when fed a high-fat diet. Energy turnover might be increased in specific PASKIN-deficient cell types under distinct environmental conditions. According to the current model, binding of a putative ligand to the PAS domain disinhibits the kinase domain and activates PASKIN auto- and target phosphorylation. Future research needs to be conducted to elucidate the nature of the putative ligand and the molecular mechanisms of downstream signalling by PASKIN.

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8 citations in Web of Science®
8 citations in Scopus®
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Additional indexing

Item Type:Journal Article, refereed, further contribution
Communities & Collections:04 Faculty of Medicine > Center for Integrative Human Physiology
04 Faculty of Medicine > Institute of Physiology
07 Faculty of Science > Institute of Physiology
DDC:570 Life sciences; biology
610 Medicine & health
Language:English
Date:2009
Deposited On:22 Jun 2009 14:35
Last Modified:27 Nov 2013 21:41
Publisher:Springer
ISSN:1420-682X
Funders:Wolfermann-Nägeli-Stiftung, Baugarten Stiftung/Stiftung für wissenschaftl. Forschung an der Universität Zürich, Swiss National Science Foundation
Additional Information:The original publication is available at www.springerlink.com
Publisher DOI:10.1007/s00018-009-8699-0
PubMed ID:19189049

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