A-Kinase Anchoring Protein AKAP220 Binds to Glycogen Synthase Kinase-3β (GSK-3β) and Mediates Protein Kinase A-dependent Inhibition of GSK-3β*
By C. Tanji, Hideki Yamamoto, N. Yorioka, N. Kohno, K. Kikuchi, A. Kikuchi. Journal of Biological Chemistry, 2002
119 citations recorded by the source corpus.
Glycogen synthase kinase-3 (GSK-3) is regulated by various extracellular ligands and phosphorylates many substrates, thereby regulating cellular functions. Using yeast two-hybrid screening, we found that GSK-3β binds to AKAP220, which is known to act as an A-kinase anchoring protein. GSK-3β formed a complex with AKAP220 in intact cells at the endogenous level. Cyclic AMP-dependent protein kinase (PKA) and type 1 protein phosphatase (PP1) were also detected in this complex, suggesting that AKAP220, GSK-3β, PKA, and PP1 form a quaternary complex. It has been reported that PKA phosphorylates GSK-3β, thereby decreasing its activity. When COS cells were treated with dibutyryl cyclic AMP to activate PKA, the activity of GSK-3β bound to AKAP220 decreased more markedly than the total GSK-3β activity. Calyculin A, a protein phosphatase inhibitor, also inhibited the activity of GSK-3β bound to AKAP220 more strongly than the total GSK-3β activity. These results suggest that PKA and PP1 regulate the activity of GSK-3β efficiently by forming a complex with AKAP220.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/321ea86afef511d2e25e7db18c403a709eba19e4
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Citations in the corpus
- AKAP signalling complexes: focal points in space and time (2004, background): “pl?Q9UKA4">AKAP220 , which assembles a complex containing PKA, PP1 and glycogen synthase kinase-3β (GSK3β), a serine/threonine kinase from the Wnt pathwa”
- GSK-3: tricks of the trade for a multi-tasking kinase (2003, background): “In addition, a yeast two-hybrid screen identified the A-kinaseanchoring protein AKAP220 as a GSK-3-binding partner (Tanji et al., 2002).”