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The type II cAMP-dependent protein kinase (PKA) is a multifunctional kinase with a broad range of substrates. Specificity of PKA signaling is mediated by the compartmentalization of the kinase to specific sites within the cell. To maintain this specific localization, the R subunit (RII) of PKA interacts with specific RII-anchoring proteins, designated A-kinase anchoring proteins (AKAP). AKAP 3, also known as AKAP 110, FSP95, PRKA3 and SOB1, binds both PKA and PDE4A and functions as a scaffolding protein in spermatozoa to regulate local cAMP concentrations and modulate sperm functions. Expression of AKAP 3 in normal tissues is restricted to the testis, where bicarbonate stimulates tyrosine phosphorylation of AKAP 3, thereby increasing its recruitment of PKA. AKAP-3 also exhibits high expression in patients with epithelial ovarian cancer (EOC). It demonstrates tumor-restricted expression and appears to be associated with worse overall survival, which make AKAP 3 a potential target for antigen-specific immunotherapy in EOC.
A kinase (PRKA) anchor protein 3; AKAP 110; AKAP110; Akap3; AKAP-3; A-kinase anchor protein 110 kDa; A-kinase anchor protein 3; A-kinase anchor protein, 110kDa; A-kinase anchoring protein 3; Cancer/testis antigen 82; CT82; epididymis luminal protein 159; Fibrous Sheath Protein of 95 kDa; fibrousheathin 1; Fibrousheathin I; fibrousheathin-1; FSP95; HEL159; PRKA3; protein kinase A binding protein AKAP 110; Protein kinase A-anchoring protein 3; SOB1; Sperm oocyte-binding protein; sperm oocyte-binding protein 1
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