Activation of RAC-protein kinase by heat shock and hyperosmolarity stress through a pathway independent of phosphatidylinositol 3-kinase.
- 23 July 1996
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 93 (15), 7639-7643
- https://doi.org/10.1073/pnas.93.15.7639
Abstract
RAC protein kinase (RAC-PK), a serine/threonine protein kinase containing a pleckstrin homology (PH) domain, was activated by cellular stress such as heat shock and hyperosmolarity. Wortmannin, which is known as a potent inhibitor of phosphatidylinositol 3-kinase and normally inhibits growth factor-induced activation of RAC-PK, did not suppress heat-shock induced activation of RAC-PK, indicating that this stress-induced activation of the kinase is not mediated by phosphatidylinositol 3-kinase. The PH domain was indispensable for stress-induced activation of RAC PK. In heat-treated cells, PKC delta, a member of the protein kinase C family, was found to associate with the PH domain of RAC-PK. This PKC subspecies was phosphorylated in vitro by RAC-PK. The results suggest that RAC-PK may play a role in the cellular response to stress through its PH domain.Keywords
This publication has 36 references indexed in Scilit:
- Molecular Cloning and Characterization of a New Member of the RAC Protein Kinase Family: Association of the Pleckstrin Homology Domain of 3 Types of RAC Protein Kinase with Protein Kinase C Subspecies and βγ Subunits of G ProteinsBiochemical and Biophysical Research Communications, 1995
- A target for Pl(3) kinaseNature, 1995
- The Pleckstrin Homology Domain of RAC Protein Kinase Associates with the Regulatory Domain of Protein Kinase C ζBiochemical and Biophysical Research Communications, 1994
- Molecular Cloning of Rat RAC Protein Kinase α and β and Their Association with Protein Kinase CζBiochemical and Biophysical Research Communications, 1994
- Three-dimensional solution structure of the pleckstrin homology domain from dynaminCurrent Biology, 1994
- Binding of PH Domains of β-Adrenergic-Receptor Kinase and β-Spectrin to WD40/β-Transducin Repeat Containing Regions of the β-Subunit of Trimeric G-ProteinsBiochemical and Biophysical Research Communications, 1994
- A MAP Kinase Targeted by Endotoxin and Hyperosmolarity in Mammalian CellsScience, 1994
- The stress-activated protein kinase subfamily of c-Jun kinasesNature, 1994
- Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucoseCell, 1986
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970