| Title: | "Newly identified stress-responsive protein kinases, Krs-1 and Krs-2" |
| Author(s): | Taylor LK; Wang HC; Erikson RL; |
| Address: | "Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA" |
| ISSN/ISBN: | 0027-8424 (Print) 1091-6490 (Electronic) 0027-8424 (Linking) |
| Abstract: | "The activation of protein kinases is a frequent response of cells to treatment with growth factors, chemicals, heat shock, or apoptosis-inducing agents. However, when several agents result in the activation of the same enzymes, it is unclear how specific biological responses are generated. We describe here two protein kinases that are activated by a subset of stress conditions or apoptotic agents but are not activated by commonly used mitogenic stimuli. Purification and cloning demonstrate that these protein kinases are members of a subfamily of kinases related to Ste20p, a serine/threonine kinase that functions early in a pheromone responsive signal transduction cascade in yeast. The specificity of Krs-1 and Krs-2 activation and their similarity to Ste20p suggest that they may function at an early step in phosphorylation events that are specific responses to some forms of chemical stress or extreme heat shock" |
| Keywords: | "3T3 Cells Amino Acid Sequence Animals Base Sequence Cell Line Cloning, Molecular DNA Primers Hot Temperature Humans Intracellular Signaling Peptides and Proteins MAP Kinase Kinase Kinases Mice Molecular Sequence Data Phosphorylation Protein Serine-Threoni;" |
| Notes: | "MedlineTaylor, L K Wang, H C Erikson, R L eng CA42580/CA/NCI NIH HHS/ CA67544/CA/NCI NIH HHS/ Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1996/09/17 Proc Natl Acad Sci U S A. 1996 Sep 17; 93(19):10099-104. doi: 10.1073/pnas.93.19.10099" |
