Key result
Mutations in the charged residues of the COOH-terminal half of yeast cofilin helix 3 result in a small defect in actin monomer interactions and map the PI(4,5)P2 binding site.
Population
Yeast cofilin and specific yeast strains
Design
Preclinical
Authors
Loading...
Maps yeast cofilin-PI(4,5)P2 site; leaves open roles in mammalian actin regulation.
Identifies specific residues in yeast cofilin responsible for actin monomer and PI(4,5)P2 binding, explaining the inhibition of actin-related activities by PI(4,5)P2.
Ojala et al. (2001) studied this question. Mutations in yeast cofilin was evaluated on Actin monomer and PI(4,5)P2 binding. Mutations in the charged residues of the COOH-terminal half of yeast cofilin helix 3 result in a small defect in actin monomer interactions and map the PI(4,5)P2 binding site.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: