Hsp90 and developmental networks.
The most abundant cytoplasmic chaperone of eukaryotic cells, Hsp90 is a hub in developmental regulatory networks and the first example described of the phenomenon of molecular buffering. As a chaperone for many different signaling proteins, Hsp90 maintains the clarity and strength of communication within and between cells, concealing developmental and stochastic variations that otherwise cause abrupt morphological changes in a large variety of organisms, including Drosophila and Arabidopsis. The chapter provides a framework for understanding how Hsp90 controls the sudden appearance of novel morphologies. We start with a discussion of the longstanding problem of hidden polygenic variation and then introduce the idea of signal transduction thresholds in mediating the effect of Hsp90 on the expression of phenotypic variation. This leads to a discussion of the role of nonlinearity in creating thresholds for sudden changes in cellular responses to developmental signals. We end with speculation on the potentially pivotal role of Hsp90 in controlling the developmental networks that determine morphological stasis and change in evolution.
Rutherford
Suzannah
S
Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Mailstop A2-168, 1100 Fairview Avenue North, Seattle, Washington 98109-1024, USA. srutherf@fhcrc.org
Knapp
Jennifer R
JR
Csermely
Peter
P
D000818:Animals; D014644:Genetic Variation; D018841:HSP90 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D015398:Signal Transduction
D018841:HSP90 Heat-Shock Proteins