Control of actin dynamics in cell motility.
Actin polymerization plays a major role in cell movement. The controls of actin sequestration/desequestration and of filament turnover are two important features of cell motility. Actin binding proteins use properties derived from the steady-state monomer-polymer cycle of actin in the presence of ATP, to control the F-actin/G-actin ratio and the turnover rate of actin filaments. Capping proteins and profilin regulate the size of the pools of F-actin and unassembled actin by affecting the steady-state concentration of ATP-G-actin. At steady state, the treadmilling cycle of actin filaments is fed by their disassembly from the pointed ends. It is regulated in two different ways by capping proteins and ADF, as follows. Capping proteins, in decreasing the number of growing barbed ends, increase their individual rate of growth and create a "funneled" treadmilling process. ADF/cofilin, in increasing the rate of pointed-end disassembly, increases the rate of filament turnover, hence the rate of barbed-end growth. In conclusion, capping proteins and ADF cooperate to increase the rate of actin assembly up to values that support the rates of actin-based motility processes.
Carlier
M F
MF
Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, Gif-sur-Yvette, France.
Pantaloni
D
D
D051339:Actin Depolymerizing Factors; D000199:Actins / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002465:Cell Movement; D051345:Destrin; D006801:Humans; D008840:Microfilament Proteins / Q000378:metabolism; D008958:Models, Molecular; D009419:Nerve Tissue Proteins / Q000378:metabolism
D051339:Actin Depolymerizing Factors; D000199:Actins; C495824:DSTN protein, human; D051345:Destrin; D008840:Microfilament Proteins; D009419:Nerve Tissue Proteins; D000255:Adenosine Triphosphate