alpha-Actinins are widely expressed cytoskeletal proteins that cross-link actin filaments through anti-parallel homodimers of the rod domains. Four alpha-actinin genes have been discovered in humans with alpha-actinin 1 and 4 being widely expressed in non-muscle cells. alpha-Actinins contain three conserved domains that include an N-terminal actin binding domain, four spectrin-like repeats in the central region, and a C-terminal calmodulin binding domain. alpha-Actinin cross-links the actin filament networks and associates the network to focal adhesion sites through binding of talin and vinculin. alpha-Actinin 1 is phosphorylated at Tyr-12 by FAK, while alpha-actinin 4 can be phosphorylated at Tyr-4 and Tyr-31 after EGF treatment. Tyr-4 and Tyr-31 phosphorylation inhibit actin binding and reduces actin-filament driven multi-nucleation in rat kidney cells. Thus, phosphorylation in alpha-actinins may be important for regulating actin binding and actin cytoskeletal remodeling.
alpha-Actinins are widely expressed cytoskeletal proteins that cross-link actin filaments through anti-parallel homodimers of the rod domains. Four alpha-actinin genes have been discovered in humans with alpha-actinin 1 and 4 being widely expressed in non
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