Ohta Y, Nishida E, Sakai H
FEBS Lett. 1986 Nov 24;208(2):423-6. doi: 10.1016/0014-5793(86)81061-4.
Multifunctional type II Ca2+/calmodulin-dependent protein kinase purified from rat brain cytosol was found to bind to actin filaments in vitro. The binding was saturable, and the dissociation constant for the binding was determined to be about 4 X 10(-8)M. Electron microscopic observation indicated that the kinase binds to the side of actin filaments. Calmodulin inhibited the binding of the kinase to actin filaments in a Ca2+-dependent manner. The Ca2+/calmodulin-regulated binding of the kinase to actin filaments revealed here may be important for the substrate recognition of the kinase.
从大鼠脑细胞溶胶中纯化得到的多功能Ⅱ型钙调蛋白依赖性蛋白激酶在体外被发现可与肌动蛋白丝结合。这种结合具有饱和性,结合的解离常数测定为约4×10⁻⁸M。电子显微镜观察表明,该激酶结合在肌动蛋白丝的侧面。钙调蛋白以Ca²⁺依赖的方式抑制该激酶与肌动蛋白丝的结合。此处揭示的该激酶受Ca²⁺/钙调蛋白调节的与肌动蛋白丝的结合可能对激酶的底物识别很重要。