High impact information on PPP1R1A

• Prefrontal cortical functioning depends on D1 family receptors and their complex signal transduction cascade, including protein phosphatase-1 (PP1) [1].
• Laminar and columnar organization of immunoreactivity for calcineurin, a calcium- and calmodulin-regulated protein phosphatase, in monkey striate cortex [2].
• Treatment of the immunoprecipitated material with protein phosphatase 2A shifted the mobilities of the 28- to 35-kDa polypeptides to the 26-kDa position, suggesting that the slower electrophoretic mobility was caused by phosphorylation [3].
• To better understand spinophilin's role in targeting protein phosphatase-1 within neurons, we used a combination of preembedding immunoperoxidase and postembedding immunogold labeling and electron microscopy to determine the localization of this scaffolding protein in macaque prefrontal cortex [4].
• In particular, protein phosphatase-1 mediates dopamine's actions on a variety of substrates, including glutamate receptors, and this, in turn, depends on the binding of protein phosphatase-1 to its binding protein spinophilin [4].

Biological context of PPP1R1A

• Exposure of mammalian oocytes to the protein phosphatase (PP)-1 (PP1) and PP2A inhibitor okadaic acid (OA) stimulates oocyte meiosis [5].

Anatomical context of PPP1R1A

• We have examined and quantified in primate prefrontal cortex the subcellular distribution of two isoforms of protein phosphatase-1 (PP1), PP1 alpha and PP1 gamma 1, which are components of the signal transduction pathway accessed by the D(1) dopamine receptor [6].

Associations of PPP1R1A with chemical compounds

• Inhibition of either protein phosphatase-1 (PP1) or protein phosphatase-2A (PP2A) could be responsible for this motility stimulation, since both of these phosphatases are sensitive to nanomolar quantities of CA [7].
• The regulation of glycogen synthase (GS) and glycogen phosphorylase (GP) activity by phosphorylation/ dephosphorylation has been proposed to be via changes in activities of several different protein (serine/threonine) phosphatases and kinases, including protein phosphatase (PP) 1/2A, PP2C, and cAMP-dependent protein kinase (PKA) [8].

Other interactions of PPP1R1A

• Relationship of glycogen synthase and glycogen phosphorylase to protein phosphatase 2C and cAMP-dependent protein kinase in liver of obese rhesus monkeys [8].

References