DARPP-32 is dephosphorylated on Thr75 by PP2A

Stable Identifier
R-HSA-201790
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
17535922 The B''/PR72 subunit mediates Ca2+-dependent dephosphorylation of DARPP-32 by protein phosphatase 2A

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

Proc Natl Acad Sci U S A 2007
12065642 Regulation of DARPP-32 dephosphorylation at PKA- and Cdk5-sites by NMDA and AMPA receptors: distinct roles of calcineurin and protein phosphatase-2A

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

J Neurochem 2002
Participants
Participant Of
hasEvent
Catalyst Activity
Catalyst Activity
Title
protein serine/threonine phosphatase activity of PP2A-ABdeltaC complex [cytosol]
Physical Entity
Activity
Orthologous Events
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Created