Premium
Tyrosine hydroxylase phosphorylation in vivo
Author(s) -
Dunkley Peter R.,
Dickson Phillip W.
Publication year - 2019
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/jnc.14675
Subject(s) - phosphorylation , tyrosine hydroxylase , in vivo , protein phosphorylation , adrenal medulla , phosphatase , serine , biology , kinase , tyrosine 3 monooxygenase , microbiology and biotechnology , biochemistry , chemistry , protein kinase a , enzyme , endocrinology , catecholamine
Tyrosine hydroxylase ( TH ) is the rate‐limiting enzyme in the synthesis of the catecholamines dopamine, noradrenaline and adrenaline. One of the major mechanisms for controlling the activity of TH is protein phosphorylation. TH is phosphorylated at serine residues 8, 19, 31 and 40. There have been a number of previous reviews focused on TH phosphorylation in vitro and in situ . This review on TH phosphorylation in vivo has three main sections focusing on: (1) the methods used to investigate TH phosphorylation in vivo , including the animals used, the sacrifice procedures, the tissue preparation, the measurement of TH protein levels and TH phosphorylation and the measurement of TH activation. (2) The regulation of TH phosphorylation and its consequences in vivo , including the kinases and phosphatases acting on TH , the stoichiometry of TH phosphorylation, the proteins that bind TH and TH subcellular location. (3) The acute and prolonged TH phosphorylation changes in specific catecholaminergic tissues, including the adrenal medulla, the nigrostriatal pathway and the mesolimbic pathway.