Phosphatidylinositol 4,5-Bisphosphate (PIP2)-enhanced G Protein-coupled Receptor Kinase (GRK) Activity: LOCATION, STRUCTURE, AND REGULATION OF THE PIP2 BINDING SITE DISTINGUISHES THE GRK SUBFAMILIES
Open Access
- 1 October 1996
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 271 (40) , 24907-24913
- https://doi.org/10.1074/jbc.271.40.24907
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Characterization of the G Protein-coupled Receptor Kinase GRK4Published by Elsevier ,1996
- High Affinity Binding of β-Adrenergic Receptor Kinase to Microsomal MembranesJournal of Biological Chemistry, 1996
- Lipid-mediated Regulation of G Protein-coupled Receptor Kinases 2 and 3Published by Elsevier ,1995
- Protein regulation by phosphatidylinositol lipidsChemistry & Biology, 1995
- Structure of the pleckstrin homology domain from β-spectrinNature, 1994
- Solution structure of a pleckstrin-homology domainNature, 1994
- Role of acidic amino acids in peptide substrates of the .beta.-adrenergic receptor kinase and rhodopsin kinaseBiochemistry, 1991
- G protein .beta..gamma. subunits from bovine brain and retina: equivalent catalytic support of ADP-ribosylation of .alpha. subunits by pertussis toxin but differential interactions with Gs.alpha.Biochemistry, 1989
- Mammalian .beta.2-adrenergic receptor: purification and characterizationBiochemistry, 1984
- Pure β-adrenergic receptor: the single polypeptide confers catecholamine responsiveness to adenylate cyclaseNature, 1983