In situ observation on hierarchical actin bundle network

Masui, Tomomi; Shikinaka, Kazuhiro*; Kwon, H.*; Koizumi, Satoshi; Hashimoto, Takeji; Iwase, Hiroki; Kakugo, Akira*; Gong, J.*

no journal, , 

Actin is one of the most abundant cytoskeleton proteins in eucaryotic cell. They play a crucialrole in cell motility by polymerizing monomeric globular G-actin into polymeric filamentous actin (F-actin). With actin-binding proteins (ABPs), they form higher order structures such as linear bundles, two-dimensional networks and three-dimensional gels. It has been considered that these structures are controlled by ABPs. However recent study have shown that the only one kind of artificial cationic polymer can form variety of structures depending its concentration and salt concentration. This system is a good model to elucidate the mechanism of regulation of actin and ABPs complex structure. Based on these backgrounds, we have investigated the effects of salt concentration on the stability and structure of actin-polycation complexes by using small angle neutron scattering (SANS) technique.