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• W2023346004 abstract "There are 11 known phosphodiesterase (PDE) gene families, each with their own distinct characteristics. The phosphodiesterases share the same organizational structure. Each protein has an N-terminal domain that confers regulatory properties to the protein, followed by a more C-terminal ∼270 amino acid catalytic domain and a short C-terminal tail. The sequence identity in the catalytic domain between genes is only about 35 percent, yet all PDEs possess the signature sequence H-D-X2-H-X4-N. The substrate specificities of the different PDE families run the gamut from dual-specificity PDEs to those that are highly specific for either cAMP or cGMP. The PDE1 proteins have two Ca2+/calmodulin binding domains, and binding of calmodulin to these PDEs stimulates their activity. The PDE2, PDE5, PDE6, PDE10, and PDE11 proteins all have allosteric, cyclic nucleotide-binding domains known to be part of the larger GAF domain family. The PDE4 family, a large family of enzymes with four genes and many splice variants, is responsible for the majority of basal cAMP-hydrolyzing activity in many cell types. Different PDEs are subject to protein phosphorylation by a variety of kinases that can alter PDE activity. In pancreatic β cells, PDE3B can be phosphorylated and activated by PKB in response to leptin stimulation. Various members of the PDE4 family can be phosphorylated and regulated by PKA and ERK. PDE5 can be phosphorylated by PKG, stabilizing it ability to bind and be activated by cGMP. The PDE superfamily comprises a complex set of enzymes that can provide cross-talk between the cGMP and cAMP pathways, and with Ca2+/CaM-dependent pathways and various kinase pathways, and allow the cell exquisite control of cyclic nucleotide dynamics." @default.
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• W2023346004 date "2010-01-01" @default.
• W2023346004 modified "2023-10-14" @default.
• W2023346004 title "Phosphodiesterase Families" @default.
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