Coghlan V M, Bergeson S E, Langeberg L, Nilaver G, Scott J D
Vollum Institute of Advanced Biomedical Research, Oregon Health Sciences University, Portland 97201.
Mol Cell Biochem. 1993 Nov;127-128:309-19. doi: 10.1007/978-1-4615-2600-1_28.
The cAMP-dependent protein kinase (PKA) regulates a variety of diverse biochemical events through the phosphorylation of target proteins. Because PKA is a multifunctional enzyme with a broad substrate specificity, its compartmentalization may be a key regulatory event in controlling which particular target substrates are phosphorylated. In recent years it has been demonstrated that differential localization of the type II holoenzyme is directed through interaction of the regulatory subunit (RII) with a family of A-Kinase Anchoring Proteins (AKAPs). In this report, we review evidence for PKA compartmentalization and discuss the structural and functional properties of AKAPs.
环磷酸腺苷（cAMP）依赖性蛋白激酶（PKA）通过对靶蛋白的磷酸化作用来调节各种不同的生化事件。由于PKA是一种具有广泛底物特异性的多功能酶，其区室化可能是控制哪些特定靶底物被磷酸化的关键调节事件。近年来，已经证明II型全酶的差异定位是通过调节亚基（RII）与A激酶锚定蛋白（AKAPs）家族的相互作用来实现的。在本报告中，我们综述了PKA区室化的证据，并讨论了AKAPs的结构和功能特性。
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