Binding of gelsolin domain 2 to actin. An actin interface distinct from that of gelsolin domain 1 and from ADF/cofilin.

It is generally assumed that of the six domains that comprise gelsolin, domain 2 is primarily responsible for the initial contact with the actin filament that will ultimately result in the filament being severed. Other actin-binding regions within domains 1 and 4 are involved in gelsolin's severing and subsequent capping ...
activity. The overall fold of all gelsolin repeated domains are similar to the actin depolymerizing factor (ADF)/cofilin family of actin-binding proteins and it has been proposed that there is a similarity in the actin-binding interface. Gelsolin domains 1 and 4 bind G-actin in a similar manner and compete with each other, whereas domain 2 binds F-actin at physiological salt concentrations, and does not compete with domain 1. Here we investigate the domain 2 : actin interface and compare this to our recent studies of the cofilin : actin interface. We conclude that important differences exist between the interfaces of actin with gelsolin domains 1 and 2, and with ADF/cofilin. We present a model for F-actin binding of domain 2 with respect to the F-actin severing and capping activity of the whole gelsolin molecule.
Mesh Terms:
Actin Depolymerizing Factors, Actins, Animals, Binding Sites, Binding, Competitive, Cross-Linking Reagents, Destrin, Gelsolin, Humans, Macromolecular Substances, Microfilament Proteins, Models, Molecular, Protein Folding, Protein Structure, Tertiary, Rabbits, Recombinant Proteins, Spectrometry, Fluorescence, Spectroscopy, Fourier Transform Infrared
Eur. J. Biochem.
Date: Dec. 01, 2001
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