Metazoan Hsp70 machines use Hsp110 to power protein disaggregation (Q34300523)

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13 February 2020

title

Metazoan Hsp70 machines use Hsp110 to power protein disaggregation (English)

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13 February 2020

2

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13 February 2020

Nadinath B Nillegoda

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13 February 2020

Bernd Bukau

7

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13 February 2020

1

Heike Rampelt

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13 February 2020

author name string

Kang Chi

4

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13 February 2020

Sebastian R Scholz

5

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13 February 2020

Richard I Morimoto

6

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13 February 2020

language of work or name

English

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publication date

18 September 2012

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13 February 2020

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13 February 2020

volume

31

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issue

21

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13 February 2020

page(s)

4221-4235

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describes a project that uses

13 February 2020

ImageJ

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11 June 2022

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inferred from PubMed Central ID database lookup

cites work

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Loss of Hsp110 Leads to Age-Dependent Tau Hyperphosphorylation and Early Accumulation of Insoluble Amyloid β

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The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110.

6 July 2018

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Discovery and characterization of a mammalian amyloid disaggregation activity

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Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation

6 July 2018

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Disaggregases in 4 dimensions

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A kinetic assessment of the C. elegans amyloid disaggregation activity enables uncoupling of disassembly and proteolysis

6 July 2018

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Structural and functional diversity among eukaryotic Hsp70 nucleotide exchange factors.

6 July 2018

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Destabilizing protein polymorphisms in the genetic background direct phenotypic expression of mutant SOD1 toxicity

6 July 2018

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6 July 2018

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Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation.

6 July 2018

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Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity

6 July 2018

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Functional divergence between co-chaperones of Hsc70.

6 July 2018

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6 July 2018

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6 July 2018

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Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding

6 July 2018

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Multiple 40-kDa heat-shock protein chaperones function in Tom70-dependent mitochondrial import.

6 July 2018

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Fluorescence lifetime imaging to detect actomyosin states in mammalian muscle sarcomeres.

6 July 2018

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Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: clues to a possible strategy for treating ALS.

6 July 2018

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Opposing activities protect against age-onset proteotoxicity

6 July 2018

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Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s

6 July 2018

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Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor

6 July 2018

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Progressive disruption of cellular protein folding in models of polyglutamine diseases.

6 July 2018

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Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.

6 July 2018

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The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family

6 July 2018

1 reference

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Apg-2 has a chaperone-like activity similar to Hsp110 and is overexpressed in hepatocellular carcinomas

6 July 2018

1 reference

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BAG-1--a nucleotide exchange factor of Hsc70 with multiple cellular functions

6 July 2018

1 reference

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Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function

6 July 2018

1 reference

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Hsp105alpha suppresses the aggregation of truncated androgen receptor with expanded CAG repeats and cell toxicity

6 July 2018

1 reference

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Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p

6 July 2018

1 reference

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Hassles with taking out the garbage: aggravating aggresomes.

6 July 2018

1 reference

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Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors

6 July 2018

1 reference

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The hsp110 and Grp1 70 stress proteins: newly recognized relatives of the Hsp70s

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70

6 July 2018

1 reference

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Hsp26: a temperature-regulated chaperone

6 July 2018

1 reference

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Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

6 July 2018

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BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release.

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1.

6 July 2018

1 reference

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Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins

6 July 2018

1 reference

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A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Cloning and expression of murine high molecular mass heat shock proteins, HSP105.

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Protein disaggregation mediated by heat-shock protein Hsp104.

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Structural and functional specificity of small heat shock protein HspB1 and HspB4, two cellular partners of HspB5: role of the in vitro hetero-complex formation in chaperone activity.

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Heterooligomeric complexes formed by human small heat shock proteins HspB1 (Hsp27) and HspB6 (Hsp20).

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Protein disaggregation by the AAA chaperone ClpB involves partial threading of looped polypeptide segments.

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Hsp110 is a nucleotide-activated exchange factor for Hsp70.

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Conformational properties of aggregated polypeptides determine ClpB-dependence in the disaggregation process.

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation.

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Human and yeast Hsp110 chaperones exhibit functional differences

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104.

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104.

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70 ATPase activity

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK.

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor.

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism.

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs.

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3492728

A stress-inducible 40 kDa protein (hsp40): purification by modified two-dimensional gel electrophoresis and co-localization with hsc70(p73) in heat-shocked HeLa cells

28 October 2018

1 reference

12 December 2020

Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants

1 reference

12 December 2020

The chaperoning activity of hsp110. Identification of functional domains by use of targeted deletions

1 reference

12 December 2020

Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein

1 reference

12 December 2020

Nucleotide exchange factors for Hsp70 chaperones

1 reference

12 December 2020

Defining the requirements for Hsp40 and Hsp70 in the Hsp90 chaperone pathway

1 reference

12 December 2020

Heat shock protein 40/DjB1 is required for thermotolerance in early phase

1 reference

12 December 2020

Polyglutamine protein aggregates are dynamic

1 reference

12 December 2020

Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation

1 reference

12 December 2020

Concerted and nonconcerted evolution of the Hsp70 gene superfamily in two sibling species of nematodes

1 reference

12 December 2020

Identifiers

DOI

10.1038/EMBOJ.2012.264

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22990239 AND SRC:MED&resulttype=core&format=json

13 February 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22990239 AND SRC:MED&resulttype=core&format=json

13 February 2020

PubMed publication ID

22990239

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22990239 AND SRC:MED&resulttype=core&format=json