Biochemistry of Drebrin and Its Binding to Actin Filaments
- PMID: 28865013
- DOI: 10.1007/978-4-431-56550-5_3
Biochemistry of Drebrin and Its Binding to Actin Filaments
Abstract
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 K d 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.
Keywords: Actin; Caldesmon; Cofilin; Fascin; Myosin-II; Myosin-V; Tropomyosin; α-Actinin.
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