Control of the assembly of ATP- and ADP-Actin by formins and profilin

Article Abstract:

A study suggested that profilin and ATP hydrolysis are both required for processive elongation mediated by the formin mDia1. Total internal reflection fluorescence microscopy is used to observe directly individual actin filament polymerization in the presence of two mammalian formins (mDia1 and mDia2) and two yeast formins (Bni1p and Cdc12p).

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Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis

Article Abstract:

The demonstration of FH1-FH2 domain acceleration hydrolysis of ATP coupled to profilin-actin polymerization is presented that uses the derived free energy for processive polymerization increasing 15-fold the rate constant for profillin-actin association to barbed ends. Profillin is required for and takes part in the processive function.

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The beta-thymosin/WH2 domain: structural basis for the switch from inhibition to promotion of actin assembly

Article Abstract:

The beta-thymosin/WH2 domain has versatile regulatory properties in actin dynamics and motility. A combined biochemical functional and structural approach is used to explain the basis for the switch of a G actin binding domain from assembly inhibition to assembly promotion.

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