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NPY4R — PRKACB

Text-mined interactions from Literome

Dawson et al., Biochem Cell Biol 1999 : The previous hypothesis was that PP-1 activity among several lower eukaryotes may be regulated directly by cAMP dependent protein kinase (PKA) phosphorylation
Connor et al., Mol Cell Biol 2001 : In contrast, PKA phosphorylation was required for PP1 binding and inhibition by the N-terminal I-1 ( 1-80 ) fragment
Cai et al., J Biol Chem 2002 : We concluded that serotonin, by activating 5-HT(1A) receptors, suppress glutamatergic signaling through the inhibition of CaMKII, which is achieved by the inhibition of PKA and ensuing activation of PP1
Küntziger et al., Biochemistry 2006 : PKA binding to AKAP149 in vitro is unaffected by the presence of PKC or PP1 , and similarly, PKC binding is independent of PKA or PP1
Yong et al., J Biol Chem 2006 : However, unlike the other known MYPTs, which upon phosphorylation inhibit PP1c, PKA phosphorylation of MYPT3 resulted in PP1c activation, indicating a different mode of action
Morgan et al., Proc Natl Acad Sci U S A 2008 : Our results demonstrate that PKA in CalphaM120A mutant sperm is rapidly and reversibly inhibited by 1NM-PP1 and that this blockade has selective and time dependent effects on multiple aspects of capacitation
Yger et al., Frontiers in behavioral neuroscience 2011 : It is one of three related, PKA regulated inhibitors of protein phosphatase-1 (PP1)
Bonito-Oliva et al., Neuropharmacology 2013 : They also indicate that this effect is exerted by suppressing dephosphorylation at Ser240/244, through PKA dependent activation of DARPP-32 and inhibition of PP-1