HSP90: The Rosetta stone for cellular protein dynamics?

Diane C. DeZwaan, Brian C. Freeman

Research output: Contribution to journalReview article

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1006-1012
Number of pages7
JournalCell Cycle
Volume7
Issue number8
DOIs
StatePublished - Apr 15 2008

Keywords

  • Hsp90
  • Molecular chaperone
  • Protein dynamics
  • Telomerase
  • Telomere

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology

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