Identification of four phosphorylation sites in the N-terminal region of tyrosine hydroxylase.
Reads0
Chats0
TLDR
The data establish that the initiator methionine is removed by post-translational processing to leave pro-2 as the amino-terminus of the mature protein in tyrosine hydroxylase.About:
This article is published in Journal of Biological Chemistry.The article was published on 1986-08-15 and is currently open access. It has received 222 citations till now. The article focuses on the topics: Mitogen-activated protein kinase kinase & Tyrosine hydroxylase.read more
Citations
More filters
Book ChapterDOI
Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations.
Richard B. Pearson,Bruce E. Kemp +1 more
TL;DR: This chapter presents a table of phosphorylation site sequences for protein-serine/threonine and protein-tyrosine kinases, containing consensus phosphorylated site motifs for each enzyme.
Journal ArticleDOI
The newly synthesized selective Ca2+calmodulin dependent protein kinase II inhibitor KN-93 reduces dopamine contents in PC12h cells
Mariko Sumi,Kazutoshi Kiuchi,Tomohiko Ishikawa,Akira Ishii,Masatoshi Hagiwara,Toshiharu Nagatsu,Hiroyoshi Hidaka +6 more
TL;DR: Investigation of the inhibitory property of a newly synthesized methoxybenzenesulfonamide, KN-93, on CaMKII activity in situ and in vitro suggests that it inhibits DA formation by modulating the reaction rate of TH to reduce the Ca(2+)-mediated phosphorylation levels of the TH molecule.
Journal ArticleDOI
Calcium/calmodulin-dependent protein kinase II.
Roger J. Colbran,C. M. Schworer,Y Hashimoto,Y. L. Fong,D. P. Rich,M K Smith,Thomas R. Soderling +6 more
TL;DR: The chapter summarizes the present knowledge of CaM kinase II with the particular emphasis on the molecular mechanisms involved in the regulation of kinase activity, and reviews the literature concerning the putative physiological functions of the kinase.
Journal ArticleDOI
14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteins.
Alastair Aitken,D. B. Collinge,B. P. H. van Heusden,T. Isobe,Patrick H. Roseboom,G. Rosenfeld,Jürgen Soll +6 more
TL;DR: A family of proteins known as 14-3-3 is currently receiving increased attention by investigators studying a broad range of biological systems, including plants and invertebrates, and current thinking indicates that these proteins may function as regulators in signal transduction/phosphorylation mechanisms.
Journal ArticleDOI
Tetrahydropterin-dependent amino acid hydroxylases.
TL;DR: Reversible phosphorylation of serine residues in the regulatory domains affects the activities of all three enzymes, and phenylalanine hydroxylase is allosterically regulated by its substrates, phenylAlanine and tetrahydrobiopterin.
References
More filters
Journal ArticleDOI
Complete coding sequence of rat tyrosine hydroxylase mRNA.
TL;DR: Several clones specific for tyrosine hydroxylase have been identified from a rat PC12 library by using the previously characterized clone pTH-1.2, the most complete of which is 1758 base pairs long and covers most of the length of the mRNA.
Journal ArticleDOI
The role of protein phosphorylation in the hormonal control of enzyme activity
Journal ArticleDOI
Sequence determinants of cytosolic N-terminal protein processing
TL;DR: The residue next to the Initiator Met is the most important determinant of N-terminal processing: Lys, Arg, Leu and (in prokaryotes) Phe and Ile protect the initiator Met from being removed when next to it in the sequence; Ala, Gly, Pro, Ser, Thr and ( in eukaryotic) Val in this position cause its removal.
Journal ArticleDOI
Direct phosphorylation of brain tyrosine hydroxylase by cyclic AMP-dependent protein kinase: mechanism of enzyme activation.
TL;DR: It is proposed that the pool of native tyrosine hydroxylase is composed of a mixture of enzyme molecules in both active and probably inactive forms, that the active form is phosphorylated, and that phosphorylation produces an active form of the enzyme at the expense of an inactive one.
Journal ArticleDOI
Calcium/phospholipid-dependent protein kinase (protein kinase C) phosphorylates and activates tyrosine hydroxylase
Katherine A. Albert,Elizabeth Helmer-Matyjek,Angus C. Nairn,Thomas Müller,John W. Haycock,Lloyd A. Greene,Menek Goldstein,Paul Greengard +7 more
TL;DR: Two-dimensional phosphopeptide maps of tyrosine hydroxylase were identical whether the phosphorylation was catalyzed by protein kinase C or by the catalytic subunit of cAMP-dependentprotein kinase.