The Turn Motif Is a Phosphorylation Switch That Regulates the Binding of Hsp70 to Protein Kinase C
Open Access
- 1 August 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (35) , 31585-31592
- https://doi.org/10.1074/jbc.m204335200
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Molecular Chaperones in the Cytosol: from Nascent Chain to Folded ProteinScience, 2002
- The Phosphoinositide-dependent Kinase, PDK-1, Phosphorylates Conventional Protein Kinase C Isozymes by a Mechanism That Is Independent of Phosphoinositide 3-KinaseJournal of Biological Chemistry, 2001
- Hsp90: Chaperoning signal transductionJournal of Cellular Physiology, 2001
- The Carboxyl Terminus of Protein Kinase C Provides a Switch to Regulate Its Interaction with the Phosphoinositide-dependent Kinase, PDK-1Journal of Biological Chemistry, 2001
- Protein Kinase C μ Is Regulated by the Multifunctional Chaperon Protein p32Published by Elsevier ,2000
- Carboxyl-terminal Phosphorylation Regulates the Function and Subcellular Localization of Protein Kinase C βIIPublished by Elsevier ,1999
- Phorbol‐Ester‐Activated Protein Kinase C‐α Lacking Phosphorylation at Ser657 is Down‐Regulated by a Mechanism Involving DephosphorylationEuropean Journal of Biochemistry, 1997
- Isolation of the active form of RAC-protein kinase (PKB/Akt) from transfected COS-7 cells treated with heat shock stress and effects of phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 4,5-bisphosphate on its enzyme activityFEBS Letters, 1996
- Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase CαCurrent Biology, 1996
- Reconstitution of protein kinase C alpha function by the protein kinase C beta-I carboxy terminusMolecular and Cellular Endocrinology, 1993