Ishikawa Ryoki
School of Nursing, Gunma Prefectural College of Health Science, Maebashi, Gunma, 371-0052, Japan.
Adv Exp Med Biol. 2017;1006:37-47. doi: 10.1007/978-4-431-56550-5_3.
Drebrin is an actin-binding protein mainly expressed in developing neurons and dendritic spine in mature neurons. To understand the functions of drebrin in vivo, we must understand its molecular properties. In this chapter, I will focus on the purification and characterization of drebrin in vitro. Drebrin binds to F-actin with a stoichiometry of 1:56 with a K of 13 × 10 M and strongly inhibits the binding of other actin-binding proteins such as tropomyosin, caldesmon, fascin, α-actinin, and cofilin. It also inhibits the activities of myosin-II and myosin-V. These results are discussed in terms of the possible roles of drebrin in the stability, dynamics, and organizations of actin structures in neuronal cells.
双调蛋白是一种肌动蛋白结合蛋白，主要表达于发育中的神经元以及成熟神经元的树突棘中。为了了解双调蛋白在体内的功能，我们必须了解其分子特性。在本章中，我将重点介绍双调蛋白的体外纯化和特性分析。双调蛋白以1:5至6的化学计量比与F-肌动蛋白结合，解离常数为1至3×10⁻⁶M，并强烈抑制其他肌动蛋白结合蛋白如原肌球蛋白、钙调蛋白、丝束蛋白、α-辅肌动蛋白和丝切蛋白的结合。它还抑制肌球蛋白-II和肌球蛋白-V的活性。将根据双调蛋白在神经元细胞肌动蛋白结构的稳定性、动态变化和组织中的可能作用来讨论这些结果。
