Publications [#112869] of G Vann V. Bennett

Papers Published

1. JL Freeman, JA Pitcher, X Li, V Bennett, RJ Lefkowitz, alpha-Actinin is a potent regulator of G protein-coupled receptor kinase activity and substrate specificity in vitro., FEBS letters, NETHERLANDS, vol. 473 no. 3 (May, 2000), pp. 280-4, ISSN 0014-5793
   (last updated on 2003/02/18)

   Abstract:
   G protein-coupled receptor kinases (GRKs) phosphorylate G protein-coupled receptors, thereby terminating receptor signaling. Herein we report that alpha-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 alpha-actinin to modulate substrate specificity of the GRKs. In the presence of calmodulin and alpha-actinin, GRK5 phosphorylates soluble, but not membrane-incorporated substrates. In contrast, in the presence of PIP2 and alpha-actinin, GRK5 phosphorylates membrane-incorporated, but not soluble substrates. Thus, modulation of alpha-actinin-mediated inhibition of GRKs by PIP2 and calmodulin has profound effects on both GRK activity and substrate specificity.

   Keywords:
   Actinin • Animals • Calmodulin • Caseins • Chickens • Cyclic AMP-Dependent Protein Kinases • Phosphatidylinositol 4,5-Diphosphate • Phosphorylation • Protein-Serine-Threonine Kinases • Receptors, Adrenergic, beta-2 • Rhodopsin • Substrate Specificity • antagonists & inhibitors • beta-Adrenergic Receptor Kinase • metabolism • metabolism*