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The PAS-domain kinase PASKIN: a new sensor in energy homeostasis
- Publication Year :
- 2009
-
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
- Subjects :
- Models, Molecular
Protein Conformation
Archaeal Proteins
2804 Cellular and Molecular Neuroscience
610 Medicine & health
Protein Serine-Threonine Kinases
Biology
10052 Institute of Physiology
Fungal Proteins
1307 Cell Biology
Mice
Cellular and Molecular Neuroscience
Protein structure
Bacterial Proteins
PAS domain
Protein biosynthesis
1312 Molecular Biology
Animals
Homeostasis
Humans
Insulin
Protein Isoforms
Glycogen synthase
Molecular Biology
Metabolic Syndrome
Pharmacology
Kinase
Cell Biology
Ligand (biochemistry)
Dietary Fats
3004 Pharmacology
Protein kinase domain
Biochemistry
10076 Center for Integrative Human Physiology
1313 Molecular Medicine
biology.protein
Molecular Medicine
Phosphorylation
570 Life sciences
biology
Energy Metabolism
Signal Transduction
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....28bfa84806a74790bb13980cde8de7fa