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

146 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

Access to Document

10.1074/jbc.M113.479253

Cite this

@article{96aabfbe5a5a415e97e3973ca553be40,

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.",

author = "Mattoo, \{Rayees U.H.\} and Sharma, \{Sandeep K.\} and Smriti Priya and Andrija Finka and Pierre Goloubinoff",

year = "2013",

month = jul,

day = "19",

doi = "10.1074/jbc.M113.479253",

language = "אנגלית",

volume = "288",

pages = "21399--21411",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "29",

}

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

TY - JOUR

T1 - Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates

AU - Mattoo, Rayees U.H.

AU - Sharma, Sandeep K.

AU - Priya, Smriti

AU - Finka, Andrija

AU - Goloubinoff, Pierre

PY - 2013/7/19

Y1 - 2013/7/19

N2 - 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.

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.

UR - https://www.scopus.com/pages/publications/84880515581

U2 - 10.1074/jbc.M113.479253

DO - 10.1074/jbc.M113.479253

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

C2 - 23737532

AN - SCOPUS:84880515581

SN - 0021-9258

VL - 288

SP - 21399

EP - 21411

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 29

ER -

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

Abstract

Access to Document

Other files and links

Fingerprint

Cite this