Klauck T M, Faux M C, Labudda K, Langeberg L K, Jaken S, Scott J D
Vollum Institute, Oregon Health Sciences University, Portland, 97201, USA.
Science. 1996 Mar 15;271(5255):1589-92. doi: 10.1126/science.271.5255.1589.
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.
多价结合蛋白，如酵母支架蛋白Sterile-5，通过作为信号单元组装的平台来协调激酶的定位。同样，在哺乳动物细胞中，环磷酸腺苷依赖性蛋白激酶（PKA）和磷酸酶2B[钙调神经磷酸酶（CaN）]由A激酶锚定蛋白AKAP79复合。缺失分析和结合研究表明，第三种酶蛋白激酶C（PKC）在与PKA或CaN结合的位点不同的位置与AKAP79结合。PKC和AKAP79在神经元中的亚细胞分布相似。因此，AKAP79似乎作为三种多功能酶的支架蛋白发挥作用。
