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• W2580294831 abstract "The specificity of a substrate is determined not only by the primary sequence, but also by several other factors that affect the degree of phosphorylation of a given target. The tertiary structure of the substrate affects function and kinetics of the kinase, such as for example the catalytic subunit of cAMP-kinase that in part acquires its substrate specificity from the conserved F at position P11 -1 . The organization of the microenvironment around a phosphorylation event has a clear impact. In that respect, anchoring proteins (AKAPs, GKAPs) play an important role by locating PKA and PKG in close vicinity to their substrates and demonstrate how low-affinity substrates may become physiologically relevant. The cAMP-and cGMP-kinases (PKA and PKG, respectively) belong to the ACG-subclass of Ser/Thr-specific protein kinases and generally prefer the phosphate acceptor residue preceded by a row of basic residues. S is the favored phosphate acceptor also when taking into account the 12-fold higher frequency of S over T in eukaryotic proteins. Based on an extensive body of work with peptide substrates in vitro and mapping of phosphorylation sites in physiological substrates in vivo, PKA is well known to phosphorylate substrates with the general motif (R(R/K)X(S/T), whereas the consensus for PKG substrates is (R/K 2–3 ) (X/K)(S/T) and includes more basic residues than the PKA consensus. This chapter presents data on the total availability of PKA and PKG consensus sites in the human proteome, estimate frequencies of phosphorylation of different motifs, and attempt to give an overview of physiological substrates of both kinases that meet a set of eligibility criteria." @default.
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• W2580294831 date "2003-01-01" @default.
• W2580294831 modified "2023-09-23" @default.
• W2580294831 title "Physiological Substrates of PKA and PKG" @default.
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• W2580294831 doi "https://doi.org/10.1016/b978-012124546-7/50564-7" @default.
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