Association of protein kinase A and protein phosphatase 2B with a common anchoring protein

Coghlan, V. M., Perrino, B. A., Howard, M., Langeberg, L. K., Hicks, J. B., Gallatin, W. M., Scott, J. D. (1995) Association of protein kinase A and protein phosphatase 2B with a common anchoring protein. Science, 267 (5195). pp. 108-111. ISSN 00368075 (ISSN)

Abstract

Specificity of protein kinases and phosphatases may be achieved through compartmentalization with preferred substrates. In neurons, adenosine 3′,5′-monophosphate (cAMP)-dependent protein kinase (PKA) is localized at postsynaptic densities by association of its regulatory subunit with an A kinase anchor protein, AKAP79. Interaction cloning experiments demonstrated that AKAP79 also binds protein phosphatase 2B, or calcineurin (CaN). A ternary complex of PKA, AKAP, and CaN was isolated from bovine brain, and colocalization of the kinase and the phosphatase was established in neurites of cultured hippocampal neurons. The putative CaN-binding domain of AKAP79 is similar to that of the immunophilin FKBP-12, and AKAP79 inhibited CaN phosphatase activity. These results suggest that both PKA and CaN are targeted to subcellular sites by association with a common anchor protein and thereby regulate the phosphorylation state of key neuronal substrates.

Item Type: Paper
Uncontrolled Keywords: calcineurin cyclic amp dependent protein kinase phosphoprotein phosphatase animal tissue article brain cattle enzyme substrate hippocampus molecular cloning nerve cell nonhuman priority journal protein phosphorylation protein protein interaction synapse Amino Acid Sequence Animal Binding Sites Brain Chemistry Calmodulin-Binding Proteins Carrier Proteins Cells, Cultured Cyclic AMP-Dependent Protein Kinases Molecular Sequence Data Neurites Phosphorylation Proteins Rats Recombinant Proteins Support, U.S. Gov't, P.H.S. Tacrolimus
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein phosphatase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
CSHL Authors:
Communities: CSHL labs > Hicks lab
Depositing User: Matt Covey
Date: 1995
Date Deposited: 09 Aug 2013 20:53
Last Modified: 12 Aug 2013 15:23
Related URLs:
URI: https://repository.cshl.edu/id/eprint/28534

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