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 | |
| State | Published - Apr 15 2008 |
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Keywords
- Hsp90
- Molecular chaperone
- Protein dynamics
- Telomerase
- Telomere
ASJC Scopus subject areas
- Molecular Biology
- Developmental Biology
- Cell Biology
Cite this
HSP90 : The Rosetta stone for cellular protein dynamics? / DeZwaan, Diane C.; Freeman, Brian C.
In: Cell Cycle, Vol. 7, No. 8, 15.04.2008, p. 1006-1012.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - HSP90
T2 - The Rosetta stone for cellular protein dynamics?
AU - DeZwaan, Diane C.
AU - Freeman, Brian C
PY - 2008/4/15
Y1 - 2008/4/15
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.
KW - Hsp90
KW - Molecular chaperone
KW - Protein dynamics
KW - Telomerase
KW - Telomere
UR - http://www.scopus.com/inward/record.url?scp=43549102208&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=43549102208&partnerID=8YFLogxK
U2 - 10.4161/cc.7.8.5723
DO - 10.4161/cc.7.8.5723
M3 - Review article
C2 - 18414022
AN - SCOPUS:43549102208
VL - 7
SP - 1006
EP - 1012
JO - Cell Cycle
JF - Cell Cycle
SN - 1538-4101
IS - 8
ER -