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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-1428

Hofer, T; Spielmann, P; Stengel, P; Stier, B; Katschinski, D M; Desbaillets, I; Gassmann, M; Wenger, R H (2001). Mammalian PASKIN, a PAS-serine/threonine kinase related to bacterial oxygen sensors. Biochemical and Biophysical Research Communications (BBRC), 288(4):757-764.



The PAS domain is a versatile protein fold found in many archaeal, bacterial, and plant proteins capable of sensing environmental changes in light intensity, oxygen concentration, and redox potentials. The oxygen sensor FixL from Rhizobium species contains a heme-bearing PAS domain and a histidine kinase domain that couples sensing to signaling. We identified a novel mammalian PAS protein (PASKIN) containing a domain architecture resembling FixL. PASKIN is encoded by an evolutionarily conserved single-copy gene which is ubiquitously expressed. The human PASKIN and mouse Paskin genes show a conserved intron-exon structure and share their promoter regions with another ubiquitously expressed gene that encodes a regulator of protein phosphatase-1. The 144-kDa PASKIN protein contains a PAS region homologous to the FixL PAS domain and a serine/threonine kinase domain which might be involved in signaling. Thus, PASKIN is likely to function as a mammalian PAS sensor protein.

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 12:23
Last Modified:28 Nov 2013 00:58
Publisher DOI:10.1006/bbrc.2001.5840
PubMed ID:11688972
Citations:Web of Science®. Times Cited: 23
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