Summary
Heat shock proteins interact with multiple key components of signaling pathways that regulate growth and development. The molecular relationships between heat shock proteins, various signaling proteins and partner proteins appear to be critical for the normal function of signal transduction pathways. The relative levels of these proteins may be important, as too little or too much Hsp70 or Hsp90 can result in aberrant growth control, developmental malformations and cell death. Although the functions of heat shock proteins as molecular chaperones have been well characterized, their complementary role as a `stress-induced' proteins to monitor changes and alter the biochemical environment of the cell remains elusive. Genetic and molecular interactions between heat shock proteins, their co-chaperones and components of signaling pathways suggest that crosstalk between these proteins can regulate proliferation and development by preventing or enhancing cell growth and cell death as the levels of heat shock proteins vary in response to environmental stress or disease.
- Signal transduction
- Hsp70
- Hsp90
- Bag1
- Nuclear hormone receptors
- Kinases
- Molecular chaperones
- Protein folding
- Protein aggregation
- © The Company of Biologists Limited 2002
Article navigation
- Top
- Article
- Summary
- Too much or too little is not good
- Hsp70 and Hsp90 are heat shock proteins
- Biochemical activities of Hsp70
- Biochemical activities of Hsp90
- Interaction between chaperones and signaling molecules
- Chaperones and the Ras/Raf-1 signal transduction pathway
- Chaperones and nuclear hormone aporeceptor complex assembly
- Perspectives: consequences of variations in levels of chaperones and co-chaperones
- Acknowledgements
- References
- Figures & tables
- Info & metrics
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