HSP90: The Rosetta stone for cellular protein dynamics?

Diane C. DeZwaan; Brian C. Freeman

doi:10.4161/cc.7.8.5723

HSP90: The Rosetta stone for cellular protein dynamics?

Diane C. DeZwaan, Brian C. Freeman

Cell and Developmental Biology

Research output: Contribution to journal › Review article › peer-review

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 language	English (US)
Pages (from-to)	1006-1012
Number of pages	7
Journal	Cell Cycle
Volume	7
Issue number	8
DOIs	https://doi.org/10.4161/cc.7.8.5723
State	Published - 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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title = "HSP90: The Rosetta stone for cellular protein dynamics?",

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.",

keywords = "Hsp90, Molecular chaperone, Protein dynamics, Telomerase, Telomere",

author = "DeZwaan, {Diane C.} and Freeman, {Brian C.}",

note = "Funding Information: We are grateful to Bradley Kubick and Drs. Peter L. Jones and Phillip A. Newmark (UIUC) for their useful comments on the manuscript. D.C.D. is supported on the NIH CMB training grant and B.C.F. is supported by the Public Service grant DK074270. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.",

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PY - 2008/4/15

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N2 - 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.

AB - 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.

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KW - Protein dynamics

KW - Telomerase

KW - Telomere

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HSP90: The Rosetta stone for cellular protein dynamics?

Abstract

Keywords

ASJC Scopus subject areas

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