title: Force of an actin spring.
abstract: Cellular movements are produced by forces. Typically, cytoskeletal proteins such as microtubules and actin filaments generate forces via polymerization or in conjunction with molecular motors. However, the fertilization of a Limulus polyphemus egg involves a third type of actin-based cellular engine--a biological spring. During the acrosome reaction, a 60-microm long coiled and twisted bundle of actin filaments straightens and extends from a sperm cell, penetrating the vitelline layer surrounding the egg. A subtle overtwist of 0.2 degrees /subunit underlies the mechanochemical basis for the extension of this actin spring. Upon calcium activation, this conformational strain energy is converted to mechanical work, generating the force required to extend the bundle through the vitelline layer. In this article, we stall the extension of the acrosome bundle in agarose gels of different concentrations. From the stall forces, we estimate a maximum force of 2 nN and a puncturing pressure of 1.6 MPa. We show the maximum force of extension is three times larger than the force required to puncture the vitelline layer. Thus, the elastic strain energy stored in the acrosome bundle is more than sufficient to power the acrosome reaction through the egg envelope.
authors.affiliation: Department of Mechanical Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
authors.forename: Jennifer H
authors.initials: JH
authors.lastname: Shin
authors.forename: Barney K
authors.initials: BK
authors.lastname: Tam
authors.forename: Ricardo R
authors.initials: RR
authors.lastname: Brau
authors.forename: Matthew J
authors.initials: MJ
authors.lastname: Lang
authors.forename: L
authors.initials: L
authors.lastname: Mahadevan
authors.forename: Paul
authors.initials: P
authors.lastname: Matsudaira
mesh_terms: D000199:Actins / Q000737:chemistry* / Q000648:ultrastructure*; D003198:Computer Simulation; D004548:Elasticity; D008956:Models, Chemical; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D009038:Motion; D013314:Stress, Mechanical
chemical_list: D000199:Actins; D020409:Molecular Motor Proteins