The Role of Electrostatic Interactions in the Regulation of the Membrane Association of G Protein βγ Heterodimers
Open Access
- 1 November 2001
- journal article
- Published by Elsevier BV
- Vol. 276 (48), 45153-45159
- https://doi.org/10.1074/jbc.m101784200
Abstract
No abstract availableThis publication has 57 references indexed in Scilit:
- Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteinsBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1999
- New Insights into the Interaction of Ras with the Plasma MembraneCell, 1999
- Understanding covalent modifications of proteins by lipids: where cell biology and biophysics mingleTrends in Cell Biology, 1997
- Binding of prenylated and polybasic peptides to membranes: affinities and intervesicle exchangeBiochemistry, 1995
- The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactionsTrends in Biochemical Sciences, 1995
- Lipid Modifications of Trimeric G ProteinsPublished by Elsevier BV ,1995
- Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids.Proceedings of the National Academy of Sciences of the United States of America, 1994
- Roles of Lipid Modifications of Transducin Subunits in Their GDP-Dependent Association and Membrane BindingBiochemistry, 1994
- A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membraneCell, 1990
- The src protein contains multiple domains for specific attachment to membranes.Molecular and Cellular Biology, 1990