Guanylyl cyclase structure, function and regulation
نویسندگان
چکیده
منابع مشابه
Regulation of soluble guanylyl cyclase by phosphorylation
Results In vitro kinase assays revealed that the α1, but not the β1, subunit of sGC is a PKG substrate and that the phosphorylation site is located within the first 360 residues of the α1. A constitutively active form of PKG stimulated incorporation of 32P into the α1 subunit in vivo. In addition, PKG could be detected in sGC immunoprecipitates, suggesting that the two proteins interact in cell...
متن کاملCrystal structure of the guanylyl cyclase Cya2.
Cyclic GMP (cGMP) is an important second messenger in eukaryotes. It is formed by guanylyl cyclases (GCs), members of the nucleotidyl cyclases class III, which also comprises adenylyl cyclases (ACs) from most organisms. To date, no structures of eukaryotic GCs are available, and all bacterial class III proteins were found to be ACs. Here we describe the biochemical and structural characterizati...
متن کاملThe regulation and physiological roles of the guanylyl cyclase receptors.
CYCLIC guanosine 3', 5'-monophosphate (cGMP) was the second of the cyclic nucleotide "second messengers" discovered [1-3] and 35 years later, its role in many cells remains unclear. It has been suggested that the rate of cGMP turnover is one means by which this nucleotide signals [4], but most studies suggest cells monitor intracellular cGMP concentrations, which are regulated by guanylyl cycla...
متن کاملHuman recombinant soluble guanylyl cyclase: expression, purification, and regulation.
The alpha1- and beta1-subunits of human soluble guanylate cyclase (sGC) were coexpressed in the Sf9 cells/baculovirus system. In addition to the native enzyme, constructs with hexahistidine tag at the amino and carboxyl termini of each subunit were coexpressed. This permitted the rapid and efficient purification of active recombinant enzyme on a nickel-affinity column. The enzyme has one heme p...
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ژورنال
عنوان ژورنال: Cellular Signalling
سال: 2011
ISSN: 0898-6568
DOI: 10.1016/j.cellsig.2011.09.001