Identification of a Structural Element in Phospholipase C β2 That Interacts with G Protein βγ Subunits
Open Access
- 1 March 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (12) , 7148-7154
- https://doi.org/10.1074/jbc.273.12.7148
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- REGULATION OF EUKARYOTIC PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C AND PHOSPHOLIPASE DAnnual Review of Biochemistry, 1997
- Phospholipase C β2 Association with Phospholipid Interfaces Assessed by Fluorescence Resonance Energy TransferJournal of Biological Chemistry, 1996
- 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
- Crystal structure of a mammalian phosphoinositide-specific phospholipase CδNature, 1996
- Phospholipase C δ1 requires a pleckstrin homology domain for interaction with the plasma membraneBiochemical Journal, 1995
- Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain.Proceedings of the National Academy of Sciences, 1995
- PH domains and phospholipases — a meaningful relationship?Trends in Biochemical Sciences, 1994
- Activation of phospholipase C beta 2 by the alpha and beta gamma subunits of trimeric GTP-binding protein.Proceedings of the National Academy of Sciences, 1993
- Regulation of phospholipase C by G proteinsTrends in Biochemical Sciences, 1992