Disease relevance of AKAP5

• The cDNA insert was ligated into the pET-3b expression plasmid, and large amounts of the partial P75 polypeptide (designated P47) were produced in Escherichia coli [1].

High impact information on AKAP5

• 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 [2].
• We have addressed these previously untested propositions by overexpressing bovine AKAP75 in a human cell line (HEK293) [3].
• Molecular characterization of bovine brain P75, a high affinity binding protein for the regulatory subunit of cAMP-dependent protein kinase II beta [1].
• Preincubation of bovine heart protein kinase II alpha and RII beta(1-50) with MAP2(31) prevented their binding to both P75 and MAP2(31) that were immobilized on nitrocellulose, suggesting that the binding sites for MAP2 and P75 are located near each other or that the same site on RII was binding to both proteins [4].
• RII-B is selectively expressed in the central nervous system, tightly associated with cerebral cortex membranes, and avidly complexed by the bovine brain calmodulin-binding protein designated P75 (Sarkar, D., Erlichman, J., and Rubin, C. S. (1984) J. Biol. Chem. 259, 9840-9846) [5].

Anatomical context of AKAP5

• We showed previously that mAKAP82, the major protein of the fibrous sheath of the mouse sperm flagellum, is an AKAP [6].
• The effect of cAMP on ROMK1 in oocytes coexpressing AKAP75 is inhibited by H89 [7].

Associations of AKAP5 with chemical compounds

• P75 was also present in high concentrations in Triton X-100 extracts prepared from cerebral cortex and liver membranes [8].

Analytical, diagnostic and therapeutic context of AKAP5

• Western blot analyses revealed that monoclonal antibody 918 exclusively bound to P75 in the brain RII preparation while monoclonal antibody 107 complexed RII [8].
• We have used the patch-clamp technique to explore the role of A Kinase Anchor Proteins (AKAP) in mediating the effect of cAMP on ROMK1 channels expressed in the Xenopus oocytes [7].

References