Coordination of Three Signaling Enzymes by AKAP79, a Mammalian Scaffold Protein

Multivalent binding proteins, such as the yeast scaffold protein Sterile-5, coordinate the location of kinases by serving as platforms for the assembly of signaling units. Similarly, in mammalian cells the cyclic adenosine 3′,5′-monophosphate-dependent protein kinase (PKA) and phosphatase 2B [calcin...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1996-03, Vol.271 (5255), p.1589-1592
Main Authors: Klauck, Theresa M., Faux, Maree C., Labudda, Kirstin, Langeberg, Lorene K., Jaken, Susan, Scott, John D.
Format: Article
Language:English
Subjects:
A Kinase Anchor Proteins
Adaptor Proteins, Signal Transducing
Amino Acid Sequence
Animals
Antibodies
Biological and medical sciences
Brain
Brain - enzymology
Calcineurin
Calmodulin - pharmacology
Calmodulin-Binding Proteins - metabolism
Carrier Proteins
Cattle
Cell Line
Cell lines
Cell physiology
Cell regulation
Cellular control mechanisms
Cyclic AMP-Dependent Protein Kinases - analysis
Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors
Cyclic AMP-Dependent Protein Kinases - metabolism
Enzymes
Fundamental and applied biological sciences. Psychology
Fungal Proteins - metabolism
HEK293 cells
Humans
Inhibition
Mammals
Medical research
Molecular and cellular biology
Molecular Sequence Data
Neurons
Neurons - chemistry
Phosphatases
Phosphoprotein Phosphatases - metabolism
Phosphorylation
Protein Kinase C - analysis
Protein Kinase C - antagonists & inhibitors
Protein Kinase C - metabolism
Protein kinases
Proteins
Proteins - analysis
Proteins - metabolism
Proteins - pharmacology
Recombinant Proteins
Saccharomyces cerevisiae Proteins
Scaffolds
Signal Transduction
Synapses - physiology
Ungulates
Yeast
Yeasts
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Summary:Multivalent binding proteins, such as the yeast scaffold protein Sterile-5, coordinate the location of kinases by serving as platforms for the assembly of signaling units. Similarly, in mammalian cells the cyclic adenosine 3′,5′-monophosphate-dependent protein kinase (PKA) and phosphatase 2B [calcineurin (CaN)] are complexed by an A kinase anchoring protein, AKAP79. Deletion analysis and binding studies demonstrate that a third enzyme, protein kinase C(PKC), binds AKAP79 at a site distinct from those bound by PKA or CaN. The subcellular distributions of PKC and AKAP79 were similar in neurons. Thus, AKAP79 appears to function as a scaffold protein for three multifunctional enzymes.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.271.5255.1589