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 1:5~6 with a Kd of 1~3 × 10−7 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.
CITATION STYLE
Ishikawa, R. (2017). Biochemistry of drebrin and its binding to actin filaments. In Advances in Experimental Medicine and Biology (Vol. 1006, pp. 37–47). Springer New York LLC. https://doi.org/10.1007/978-4-431-56550-5_3
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