α-Actinin is a potent regulator of G protein-coupled receptor kinase activity and substrate specificity in vitro

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Abstract

G protein-coupled receptor kinases (GRKs) phosphorylate G protein-coupled receptors, thereby terminating receptor signaling. Herein we report that α-actinin potently inhibits all GRK family members. In addition, calcium-bound calmodulin and phosphatidylinositol 4,5-bisphosphate (PIP2), two regulators of GRK activity, coordinate with α-actinin to modulate substrate specificity of the GRKs. In the presence of calmodulin and α-actinin, GRK5 phosphorylates soluble, but not membrane-incorporated substrates. In contrast, in the presence of PIP2 and α-actinin, GRK5 phosphorylates membrane-incorporated, but not soluble substrates. Thus, modulation of α-actinin-mediated inhibition of GRKs by PIP2 and calmodulin has profound effects on both GRK activity and substrate specificity. Copyright (C) 2000 Federation of European Biochemical Societies.

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Freeman, J. L. R., Pitcher, J. A., Li, X., Bennett, V., & Lefkowitz, R. J. (2000). α-Actinin is a potent regulator of G protein-coupled receptor kinase activity and substrate specificity in vitro. FEBS Letters, 473(3), 280–284. https://doi.org/10.1016/S0014-5793(00)01543-X

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