Mutations in the Carboxyl-terminal Domain of Phospholipase C-β1 Delineate the Dimer Interface and a Potential GαqInteraction Site
Open Access
- 1 February 2002
- journal article
- Published by Elsevier
- Vol. 277 (6) , 4294-4300
- https://doi.org/10.1074/jbc.m109612200
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- A unique fold of phospholipase C-β mediates dimerization and interaction with GαqNature Structural & Molecular Biology, 2001
- Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 ÅNature, 2001
- GTPase-Activating Proteins for Heterotrimeric G Proteins: Regulators of G Protein Signaling (RGS) and RGS-Like ProteinsAnnual Review of Biochemistry, 2000
- Crystal Structure of the Catalytic Domains of Adenylyl Cyclase in a Complex with G sα ·GTPγSScience, 1997
- REGULATION OF EUKARYOTIC PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C AND PHOSPHOLIPASE DAnnual Review of Biochemistry, 1997
- Carboxyl-terminal Fragments of Phospholipase C-β1 with Intrinsic Gq GTPase-activating Protein (GAP) ActivityPublished by Elsevier ,1996
- The Role of Carboxyl-terminal Basic Amino Acids in Gqα-dependent Activation, Particulate Association, and Nuclear Localization of Phospholipase C-β1Journal of Biological Chemistry, 1996
- Regulation of Phospholipase C-β1 by Gq and m1 Muscarinic Cholinergic ReceptorPublished by Elsevier ,1996
- Concentration of enzyme-dependent activation of PLC-β1 and PLC-β2 by Gα11 and βγ-subunitsCellular Signalling, 1995
- Phospholipase C-β1 is a GTPase-activating protein for Gq/11, its physiologic regulatorCell, 1992