Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates

Rayees U.H. Mattoo; Sandeep K. Sharma; Smriti Priya; Andrija Finka; Pierre Goloubinoff

doi:10.1074/jbc.M113.479253

Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates

Rayees U.H. Mattoo, Sandeep K. Sharma, Smriti Priya, Andrija Finka, Pierre Goloubinoff^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

135 Scopus citations

Abstract

Background: Hsp110s are considered as mere nucleotide exchange factors of the Hsp70s. Results: Human cytosolic Hsp110s can use ATP to unfold misfolded polypeptides and act as equal partner with Hsp70 to solubilize stable protein aggregates. Conclusion: Hsp110s are Hsp70-like polypeptide unfolding chaperones. Significance: Hsp110s are powerful disaggregating chaperones that can collaborate with Hsp70s to detoxify misfolding proteins in degenerative diseases.

Original language	English
Pages (from-to)	21399-21411
Number of pages	13
Journal	Journal of Biological Chemistry
Volume	288
Issue number	29
DOIs	https://doi.org/10.1074/jbc.M113.479253
State	Published - 19 Jul 2013
Externally published	Yes

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10.1074/jbc.M113.479253

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title = "Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates",

abstract = "Background: Hsp110s are considered as mere nucleotide exchange factors of the Hsp70s. Results: Human cytosolic Hsp110s can use ATP to unfold misfolded polypeptides and act as equal partner with Hsp70 to solubilize stable protein aggregates. Conclusion: Hsp110s are Hsp70-like polypeptide unfolding chaperones. Significance: Hsp110s are powerful disaggregating chaperones that can collaborate with Hsp70s to detoxify misfolding proteins in degenerative diseases.",

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Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates. / Mattoo, Rayees U.H.; Sharma, Sandeep K.; Priya, Smriti et al.
In: Journal of Biological Chemistry, Vol. 288, No. 29, 19.07.2013, p. 21399-21411.

Research output: Contribution to journal › Article › peer-review

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AU - Mattoo, Rayees U.H.

AU - Sharma, Sandeep K.

AU - Priya, Smriti

AU - Finka, Andrija

AU - Goloubinoff, Pierre

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AB - Background: Hsp110s are considered as mere nucleotide exchange factors of the Hsp70s. Results: Human cytosolic Hsp110s can use ATP to unfold misfolded polypeptides and act as equal partner with Hsp70 to solubilize stable protein aggregates. Conclusion: Hsp110s are Hsp70-like polypeptide unfolding chaperones. Significance: Hsp110s are powerful disaggregating chaperones that can collaborate with Hsp70s to detoxify misfolding proteins in degenerative diseases.

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Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates

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