DARPP-32 is dephosphorylated on Thr75 by PP2A

Stable Identifier
Reaction [transition]
Homo sapiens
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PP2A is ubiquitously expressed in eukaryotic cells, existing as a heterotrimeric enzyme composed of a 36-kDa catalytic C subunit, a 64-kDa scaffolding A subunit, and multiple regulatory B subunits. The B subunits are thought to influence enzyme activity, substrate specificity, and subcellular localization. PKA phosphorylates PP2A thereby activating the enzyme and is responsible for dopamine/cAMP-dependent dephosphorylation of Thr-75 of DARPP-32.

Literature References
PubMed ID Title Journal Year
12065642 Regulation of DARPP-32 dephosphorylation at PKA- and Cdk5-sites by NMDA and AMPA receptors: distinct roles of calcineurin and protein phosphatase-2A

Bibb, JA, Greengard, P, Matsuyama, S, Hamada, M, Higashi, H, Nairn, AC, Nishi, A

J Neurochem 2002
17535922 The B''/PR72 subunit mediates Ca2+-dependent dephosphorylation of DARPP-32 by protein phosphatase 2A

Sung, JY, McAvoy, T, Ahn, JH, Janssens, V, Greengard, P, Nairn, AC, Goris, J, Nishi, A

Proc Natl Acad Sci U S A 2007
Catalyst Activity

protein serine/threonine phosphatase activity of PP2A-ABdeltaC complex [cytosol]

Orthologous Events
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