Dopamine or biopterin deficiency potentiates phosphorylation at (40)Ser and ubiquitination of tyrosine hydroxylase to be degraded by the ubiquitin proteasome system - Kawahata, Ichiro; Ohtaku, Shiori; Tomioka, Yoshihisa; Ichinose, Hiroshi; Yamakuni, Tohru (Biochemical and biophysical research communications, 2015)
Keywords: Animals; Biopterins - analogs & derivatives; Biopterins - deficiency; Cyclic AMP-Dependent Protein Kinases - genetics; Cyclic AMP-Dependent Protein Kinases - metabolism; Cycloheximide - pharmacology; Cysteine Proteinase Inhibitors - pharmacology; Dopamine - deficiency; Gene Expression Regulation; Isoquinolines - pharmacology; Leupeptins - pharmacology; Mesencephalon - cytology; Mesencephalon - drug effects; Mesencephalon - metabolism; Neurons - cytology; Neurons - drug effects; Neurons - metabolism; PC12 Cells; Phosphorylation - drug effects; Primary Cell Culture; Proteasome Endopeptidase Complex - drug effects; Proteasome Endopeptidase Complex - metabolism; Proteolysis - drug effects; Rats; Receptors, Dopamine D2 - genetics; Receptors, Dopamine D2 - metabolism; Serine - metabolism; Signal Transduction; Sulfonamides - pharmacology; Tyrosine 3-Monooxygenase - genetics; Tyrosine 3-Monooxygenase - metabolism; Ubiquitin - genetics; Ubiquitin - metabolism; Ubiquitination - drug effects; Dopa-responsive dystonia; Ubiquitin; Tyrosine hydroxylase; Dopamine; Parkinson's disease; Proteasome