Abstract
Compared with other chaperone systems, heat shock proteins Hsp70 and Hsp90 interact with a larger variety of co-chaperone proteins that regulate their activity or aid in the folding of specific substrate proteins. Although many co-chaperones are soluble cytosolic proteins, co-chaperone domains are also found in modular adaptor proteins, which are often localized to intracellular membranes or elements of the cytoskeleton. These specialized co-chaperones include auxilin, cysteine string protein, Tom70, UNC-45 and homologs of Bag-1. The localized co-chaperones can harness the ATP-dependent mechanisms of Hsp70 and Hsp90 to do conformational work in diverse functional contexts, including vesicle secretion and recycling, protein transport and the regulated assembly and/or disassembly of protein complexes. Such flexibility is unique to the cytosolic Hsp70 and Hsp90 chaperone system.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 541-547 |
| Number of pages | 7 |
| Journal | Trends in Biochemical Sciences |
| Volume | 28 |
| Issue number | 10 |
| DOIs | |
| State | Published - Oct 2003 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
More than folding : Localized functions of cytosolic chaperones. / Young, Jason C.; Barral, José M.; Hartl, F. Ulrich.
In: Trends in Biochemical Sciences, Vol. 28, No. 10, 10.2003, p. 541-547.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - More than folding
T2 - Localized functions of cytosolic chaperones
AU - Young, Jason C.
AU - Barral, José M.
AU - Hartl, F. Ulrich
PY - 2003/10
Y1 - 2003/10
N2 - Compared with other chaperone systems, heat shock proteins Hsp70 and Hsp90 interact with a larger variety of co-chaperone proteins that regulate their activity or aid in the folding of specific substrate proteins. Although many co-chaperones are soluble cytosolic proteins, co-chaperone domains are also found in modular adaptor proteins, which are often localized to intracellular membranes or elements of the cytoskeleton. These specialized co-chaperones include auxilin, cysteine string protein, Tom70, UNC-45 and homologs of Bag-1. The localized co-chaperones can harness the ATP-dependent mechanisms of Hsp70 and Hsp90 to do conformational work in diverse functional contexts, including vesicle secretion and recycling, protein transport and the regulated assembly and/or disassembly of protein complexes. Such flexibility is unique to the cytosolic Hsp70 and Hsp90 chaperone system.
AB - Compared with other chaperone systems, heat shock proteins Hsp70 and Hsp90 interact with a larger variety of co-chaperone proteins that regulate their activity or aid in the folding of specific substrate proteins. Although many co-chaperones are soluble cytosolic proteins, co-chaperone domains are also found in modular adaptor proteins, which are often localized to intracellular membranes or elements of the cytoskeleton. These specialized co-chaperones include auxilin, cysteine string protein, Tom70, UNC-45 and homologs of Bag-1. The localized co-chaperones can harness the ATP-dependent mechanisms of Hsp70 and Hsp90 to do conformational work in diverse functional contexts, including vesicle secretion and recycling, protein transport and the regulated assembly and/or disassembly of protein complexes. Such flexibility is unique to the cytosolic Hsp70 and Hsp90 chaperone system.
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UR - http://www.scopus.com/inward/citedby.url?scp=0642377466&partnerID=8YFLogxK
U2 - 10.1016/j.tibs.2003.08.009
DO - 10.1016/j.tibs.2003.08.009
M3 - Article
VL - 28
SP - 541
EP - 547
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
SN - 0376-5067
IS - 10
ER -