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 13:23|
|Last Modified:||28 Nov 2013 01:58|
|Citations:||Web of Science®. Times Cited: 23|
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