Visual insight into how low pH alone can induce actin-severing ability in gelsolin under calcium-free conditions.

ABSTRACT: Gelsolin is a key actin cytoskeleton-modulating protein primarily regulated by calcium and phosphoinositides. In addition, low pH has also been suggested to activate gelsolin in the absence of Ca(2+) ions, although no structural insight on this pathway is available except for a reported decrement in its diffusion coefficient at low pH. We also observed ~1.6-fold decrease in the molecular mobility of recombinant gelsolin when buffer pH was lowered from 9 to 5. Analysis of the small angle x-ray scattering data collected over the same pH range indicated that the radius of gyration and maximum linear dimension of gelsolin molecules increased from 30.3 to 34.1 Å and from 100 to 125 Å, respectively. Models generated for each dataset indicated that similar to the Ca(2+)-induced process, low pH al

SUBMITTER: Garg R 

PROVIDER: S-EPMC3121526 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature