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110 kD dimer actin binding protein

Page updated 7th March '04

Isolated from Acanthamoeba castellanii (Ueno & Korn, 1986). Actually a dimer composed of two 55kDa subunits, each subunit binds one actin monomer within the filament.  No effect on the viscosity of actin filaments and slows polymerization of ADP but not ATP actin suggesting weak sequestering activity of ADP-monomers?   110kD protein is enriched in the cortex and the function of the protein may be to modulate the interaction of actin and myosin as the mysoin ATPase is inhibited by the protein.  110kDa protein enhanced the sedimentation of actin. Perhaps a caldsemon or tropomysoin like protein?  No sequence data available.

 

References:-

Uedo, T. & Korn, E.D. (1986). "Isolation and partial characterization of a 110-kD dimer actin-binding protein." J.Cell Biol. 103, 621-630.

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