The role of profilin in formin-nucleated actin cable assembly[Edit]
Profilin binds simultaneously to formin and actin monomers; this interaction tethers multiple profilin-actin complexes near the growing end of actin filaments, which promotes the processive addition of actin subunits [1, 2]. Profilin uses the energy from ATP hydrolysis generated during actin polymerization to facilitate actin assembly [2]. Profilin binds to cytoplasmic ATP-actin monomers better than cytoplasmic ADP-actin monomers [3].
Profilin has been suggested to generally increase the elongation rate of formin-associated filaments by:
* Catalyzing the exchange of ADP for ATP on actin monomers [4, 5].
* Blocking free monomers from elongating pointed ends [4].
* Lowering the critical concentration at the barbed end [2].
* Promoting the association of G-actin-ATP to the barbed end [6].
* Catalyzing the exchange of ADP for ATP on actin monomers [4, 5].
* Blocking free monomers from elongating pointed ends [4].
* Lowering the critical concentration at the barbed end [2].
* Promoting the association of G-actin-ATP to the barbed end [6].
Importantly however, profilin also promotes disassembly of actin filaments by sequestering monomeric G-actin, thereby blocking its association with the barbed ends and promoting its disassembly from the pointed ends of actin filaments [4]. The combined actions of profilin and ADF/cofilin synergize to enhance turnover of actin filaments [7].