Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractTranscriptomic Analysis of Trichoderma atroviride Overgrowing Plant-Wilting Verticillium dahliae Reveals the Role of a New M14 Metallocarboxypeptidase CPA1 in Biocontrol    Next Abstract"On the generation and outcome of 3-(N-phenylamino)propane-1,2-diol derivatives in deodorized model oils related to toxic oil syndrome" »

EMBO J


Title:The Sch9 protein kinase regulates Hsp90 chaperone complex signal transduction activity in vivo
Author(s):Morano KA; Thiele DJ;
Address:"Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109-0606, USA"
Journal Title:EMBO J
Year:1999
Volume:18
Issue:21
Page Number:5953 - 5962
DOI: 10.1093/emboj/18.21.5953
ISSN/ISBN:0261-4189 (Print) 1460-2075 (Electronic) 0261-4189 (Linking)
Abstract:"Basal and stress-induced synthesis of the components of the highly conserved heat shock protein Hsp90 chaperone complex require the heat shock transcription factor (HSF); Saccharomyces cerevisiae cells expressing the HSF allele HSF(1-583) reversibly arrest growth at 37 degrees C in the G(2)/M phase of the cell cycle due to diminished expression of these components. A suppressor mutant capable of restoring high-temperature growth to HSF(1-583) cells was identified, harboring a disruption of the SCH9 protein kinase gene, homologous to the protein kinase A and protein kinase B/Akt families of mammalian growth control kinases. Loss of Sch9 in HSF(1-583) cells derepresses Hsp90 signal transduction functions as demonstrated by restoration of transcriptional activity by the mammalian glucocorticoid receptor and the heme-dependent transcription factor Hap1, and by enhanced pheromone-dependent signaling through the Ste11 mitogen-activated protein kinase (MAPK). Moreover, Sch9-deficient cells with normal levels of Hsp90 chaperone complex components display hyperactivation of the pheromone response MAPK pathway in the absence of pheromone. These results demonstrate that the evolutionarily conserved function of the Hsp90 chaperone complex as a signal transduction facilitator is modulated by a growth regulatory kinase"
Keywords:"Carbon-Oxygen Lyases/genetics Cell Cycle/genetics *DNA-(Apurinic or Apyrimidinic Site) Lyase DNA-Binding Proteins/genetics/metabolism Fungal Proteins/metabolism Gene Expression Regulation, Fungal HSP90 Heat-Shock Proteins/*metabolism Heat-Shock Proteins/g;"
Notes:"MedlineMorano, K A Thiele, D J eng 1F32 GM19195-01/GM/NIGMS NIH HHS/ 5T32CA09676-06/CA/NCI NIH HHS/ R01 GM59911/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. England 1999/11/02 EMBO J. 1999 Nov 1; 18(21):5953-62. doi: 10.1093/emboj/18.21.5953"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 25-11-2024