Direct Binding of Syndecan-4 Cytoplasmic Domain to the Catalytic Domain of Protein Kinase Cα (PKCα) Increases Focal Adhesion Localization of PKCα
Open Access
- 1 April 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (16) , 13795-13802
- https://doi.org/10.1074/jbc.m208300200
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Solution Structure of the Dimeric Cytoplasmic Domain of Syndecan-4,Biochemistry, 2001
- Functions of Cell Surface Heparan Sulfate ProteoglycansAnnual Review of Biochemistry, 1999
- Specific Interaction of the PDZ Domain Protein PICK1 with the COOH Terminus of Protein Kinase C-αJournal of Biological Chemistry, 1997
- Multimerization of the Cytoplasmic Domain of Syndecan-4 Is Required for Its Ability to Activate Protein Kinase CJournal of Biological Chemistry, 1997
- Phosphorylation of Protein Kinase C-α on Serine 657 Controls the Accumulation of Active Enzyme and Contributes to Its Phosphatase-resistant StateJournal of Biological Chemistry, 1997
- Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase CαCurrent Biology, 1996
- Improved method for high efficiency transformation of intact yeast cellsNucleic Acids Research, 1992
- Mechanism of protein kinase C activation by phosphatidylinositol 4,5-bisphosphateBiochemistry, 1991
- Protein kinase C is localized in focal contacts of normal but not transformed fibroblastsMolecular Carcinogenesis, 1990
- Association of type 3 protein kinase C with focal contacts in rat embryo fibroblasts.The Journal of cell biology, 1989