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Review
. 2004 Sep 29;24(39):8404-9.
doi: 10.1523/JNEUROSCI.3602-04.2004.

Protein phosphatases and calcium/calmodulin-dependent protein kinase II-dependent synaptic plasticity

Roger J Colbran  1
Affiliations
Review

Protein phosphatases and calcium/calmodulin-dependent protein kinase II-dependent synaptic plasticity

Roger J Colbran. J Neurosci. .
No abstract available

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Figures

Figure 1.
Figure 1.
Multiple protein phosphatase complexes regulate CaMKII and glutamate receptors. Putative complexes of PP1 and PP2B catalytic subunits (red) and multiple kinases (green) at NMDA-type (A) and AMPA-type (B) glutamate receptors (purple) mediated by scaffolding and cytoskeletal proteins. Protein phosphatase-binding proteins are depicted in blue, whereas other scaffolding and cytoskeletal proteins are white. Phospho-proteins are indicated by the attached yellow circles. Although each protein-protein interaction has been individually demonstrated and some ternary and tertiary subcomplexes verified, complete assembly of the entire complexes has not been demonstrated. C, Regulation of soluble PP1 by phosphorylation-dephosphorylation of inhibitor-1 by PKA and PP2B, respectively. DARPP-32 (not shown) is a functional homolog of inhibitor-1 that is regulated by similar mechanisms. D, Dendritic PP2A holoenzymes. Top, Heterotrimeric PP2A holoenzymes containing the B'α regulatory subunit are inhibited by CaMKII phosphorylation. Bottom, PP2A holoenzymes containing the striatin regulatory subunit have also been localized to dendrites and PSDs.
See this image and copyright information in PMC

References

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