Activation Mechanisms of Conventional Protein Kinase C Isoforms Are Determined by the Ligand Affinity and Conformational Flexibility of Their C1 Domains
Open Access
- 1 November 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (47), 46886-46894
- https://doi.org/10.1074/jbc.m307853200
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Importance of C1B Domain for Lipid Messenger-induced Targeting of Protein Kinase CJournal of Biological Chemistry, 2002
- Roles of Ionic Residues of the C1 Domain in Protein Kinase C-α Activation and the Origin of Phosphatidylserine SpecificityJournal of Biological Chemistry, 2001
- Interplay of C1 and C2 Domains of Protein Kinase C-α in Its Membrane Binding and ActivationPublished by Elsevier ,1999
- Differential Membrane-Binding and Activation Mechanisms of Protein Kinase C-α and -εBiochemistry, 1998
- Lateral pressure in membranesBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1996
- Protein Kinase C: Seeing two domainsCurrent Biology, 1995
- Crystal structure of the Cys2 activator-binding domain of protein kinase Cδ in complex with phorbol esterCell, 1995
- Studies on the primary sequence requirements for PKC‐α, ‐β1 and ‐γ peptide substratesFEBS Letters, 1990
- Association of protein kinase C with phospholipid monolayers: two-stage irreversible bindingBiochemistry, 1988
- Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayersBiochimica et Biophysica Acta (BBA) - Biomembranes, 1975