HSP90: The Rosetta stone for cellular protein dynamics?

Diane C. DeZwaan and Brian C. Freeman

volume 7 | issue 8

15 April 2008
Pages: 1006 - 1012

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The Hsp90 proteomic network is expansive and includes a variety of cell processes operating within the cytoplasm and nucleoplasm. Though the functional significance of the extensive interactions has not been defined, we suggest that the Hsp90 molecular chaperone machinery promotes dynamic behaviors for client proteins that is critical to achieve homeostasis. A general rapid action by cell factors would permit both proper assembly of biological complexes and efficient transitions between distinct structures. Here, we describe why the properties that are inherent to molecular chaperones place these proteins in a unique position to drive the dynamic cellular environment.

Authors

Diane C. DeZwaan

University of Illinois, Urbana-Champaign; Urbana, Il

Brian C. Freeman