Vorotnikov A V, Gusev N B
Department of Biochemistry, School of Biology, Moscow State University, USSR.
FEBS Lett. 1990 Dec 17;277(1-2):134-6. doi: 10.1016/0014-5793(90)80827-6.
Taking into account the perimembrane localization of caldesmon [(1986) Nature 319, 68] and its ability to participate in the regulation of receptor clusterization [(1989) J. Biol. Chem. 264, 496], we studied the interaction of duck gizzard caldesmon with soybean phospholipids (azolectin). By using four independent methods, i.e. light scattering, gel-electrophoresis, gel-filtration and ultracentrifugation, we showed a Ca-independent complex formation between caldesmon and azolectin. Interacting with caldesmon, calmodulin is shown to dissociate the caldesmon-azolectin complex. It is supposed that the caldesmon-phospholipid interaction may affect caldesmon phosphorylation by Ca-phospholipid-dependent protein kinase. This effect may be important for various cell motility processes.
鉴于钙调蛋白的膜周定位[（1986年）《自然》319, 68]及其参与受体聚集调节的能力[（1989年）《生物化学杂志》264, 496]，我们研究了鸭肫钙调蛋白与大豆磷脂（偶氮卵磷脂）的相互作用。通过使用四种独立的方法，即光散射、凝胶电泳、凝胶过滤和超速离心，我们证明了钙调蛋白与偶氮卵磷脂之间形成了不依赖钙的复合物。钙调蛋白与钙调蛋白相互作用时，会使钙调蛋白 - 偶氮卵磷脂复合物解离。据推测，钙调蛋白 - 磷脂相互作用可能会影响钙磷脂依赖性蛋白激酶对钙调蛋白的磷酸化作用。这种作用可能对各种细胞运动过程很重要。
