F-actin, binding

In contrast, jasplakinolide, a cyclodepsipeptide from the marine sponge Jaspis johnstoni, rapidly penetrates the cell membrane. It competes with phalloidin for F-actin binding and has a dissociation constant of approximately 15 nM. It induces actin polymerization and stabilizes pre-existing actin filaments. Dolastatin 11, a depsipeptide from the mollusk Dolabella auricu-laria, induces F-actin polymerization. Its binding site differs from that of phalloidin or jasplakinolide. 

Steimle, P.A. Licate, L. Cote, G.P. Egelhoff, T.T. Lamellipodial localization of Dictyostelium myosin heavy chain kinase A is mediated via F-actin binding by the coiled-coil domain. FEBS Lett., 516, 58-62 (2002)... 

Glenney, J. R., Jr., Kaulfus, P., Matsudaira, P., and Weber, K. (1981). F-actin binding and bundling properties of fimbrin, a major cytoskeletal protein of microvillus core filaments. / Biol. Chem. 256, 9283-9288. 

Gimona, M., and Mital, R. (1998). The single CH domain of calponin is neither sufficient nor necessary for F-actin binding./. Cell Sci. Ill, 1813-1821. 

McGough, A. (1998). F-actin-binding proteins. Curr. Opin. Struct. Biol. 8, 166-176. 

Way, M., Pope, B., and Weeds, A. G. (1992). Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin Implications for the requirements of severing and capping. J. Cell Biol. 119, 835-842. 

Way, M., B. Pope, and A. Weeds. 1991. Molecular biology of actin binding proteins evidence for a common structural domain in the F-actin binding sites of gelsolin and alpha-actinin. J Cell Sci Suppl. 14 91-4. 

Cai L, Makhov AM, Bear JE. F-actin binding is essential for coronin IB function in vivo. J Cell Sci... 

Table 1 summarizes all of the known direct interactions and effects on actin of purified coronin proteins. From this compilation, it is apparent that F-actin binding and bundling are conserved functions of coronin. Arp2/3 complex and cofilin regulation by coronin may be equally well conserved, but this remains to be determined, as biochemical tests for these activities have been limited to a few studies so far. 

Vardar D, Chishti AH, Frank BS et al. Villin-type headpiece domains show a wide range of F-actin-bind-ing affinities. Cell Motil Cytoskeleton 2002 52(1) 9-21. 

In both smooth and skeletal muscles, the strong-"rigor" interaction of F-actin and myosin occurring in the absence of ATP involves F-actin binding to doubleheaded myosin with an expected 2 1 stoichiometry in both smooth and skeletal muscles (Prbchniewicz and Strzelecka-Golaszewska, 1980). 

Takahashi K, Hiwada K, Kokubu T (1986) Isolation and characterization of a 34,000-dalton calmodulin-and F-actin-binding protein from chicken gizzard smooth muscle. Biochem Biophys Res Commun 141 2026... 

Takahashi K, Hiwada K, Kokubu T (1986) Isolation and characterization of a 34,000-dalton calmodulin- and F-actin-binding protein from chicken gizzard smooth muscle. Biochem Biophys Res Commun 141 20-26 Takahashi K, Hiwada K, Kokubu T (1987) Occurrence of anti-gizzard P34K antibody cross-reactive components in bovine smooth muscles and non-smooth muscle tissues. Life Sci 41 291-296... 

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