Key result
Cofilin acts as a pH sensor mediating pH-dependent actin filament dynamics, with phosphoinositide binding being pH-dependent for wild-type cofilin but attenuated and pH-insensitive for cofilin-H133A.
Population
Fibroblasts lacking H efflux by the Na-H exchanger NHE1, and in vitro models
Comparison
Expression of mutant cofilin-H133A or… vs Wild-type cofilin and varying pH levels
Design
Preclinical
Authors
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Hypothesis-generating for pH-dependent cytoskeletal regulation; leaves open relevance to cardiovascular disease models.
Cofilin acts as a pH sensor to mediate pH-dependent actin filament dynamics through pH-dependent phosphoinositide binding involving His133.
Frantz et al. (2008) studied this question. Cofilin-H133A expression and pH changes vs. Wild-type cofilin was evaluated on Actin free barbed end formation and phosphoinositide binding. Cofilin acts as a pH sensor mediating pH-dependent actin filament dynamics, with phosphoinositide binding being pH-dependent for wild-type cofilin but attenuated and pH-insensitive for cofilin-H133A.
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