Metazoan Hsp70-based protein disaggregases: emergence and mechanisms (Q26779046)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:26501065%20AND%20SRC:MED&resulttype=core&format=json

28 February 2020

title

Metazoan Hsp70-based protein disaggregases: emergence and mechanisms (English)

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28 February 2020

1

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28 February 2020

Bernd Bukau

series ordinal

2

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28 February 2020

author name string

Nadinath B Nillegoda

series ordinal

1

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language of work or name

English

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publication date

9 October 2015

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Frontiers in molecular biosciences

28 February 2020

published in

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Crossref

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28 February 2020

volume

2

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28 February 2020

page(s)

57

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Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family

28 February 2020

cites work

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Eleven ancestral gene families lost in mammals and vertebrates while otherwise universally conserved in animals

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Hsp70 chaperones: cellular functions and molecular mechanism

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Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation

7 April 2017

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Structure of the Hsp110:Hsc70 nucleotide exchange machine

7 April 2017

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Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1

7 April 2017

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The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate

7 April 2017

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

7 April 2017

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PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone

7 April 2017

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Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1

7 April 2017

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The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding

7 April 2017

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Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1.

7 April 2017

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

7 April 2017

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

7 April 2017

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

7 April 2017

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

7 April 2017

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

7 April 2017

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

7 April 2017

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Protein disaggregation mediated by heat-shock protein Hsp104.

7 April 2017

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HSP104 required for induced thermotolerance

7 April 2017

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

7 April 2017

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Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

7 April 2017

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Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones

7 April 2017

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Nuclear localization mechanism of Hsp105beta and its possible function in mammalian cells

7 April 2017

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Different localization of Hsp105 family proteins in mammalian cells

7 April 2017

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Hsp105 but not Hsp70 family proteins suppress the aggregation of heat-denatured protein in the presence of ADP

7 April 2017

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The Hsp70 and Hsp60 chaperone machines

7 April 2017

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The cell-non-autonomous nature of electron transport chain-mediated longevity

7 April 2017

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The HSP70 chaperone machinery: J proteins as drivers of functional specificity

7 April 2017

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Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging

7 April 2017

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Opposing activities protect against age-onset proteotoxicity

7 April 2017

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Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy

7 April 2017

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Aggresomes, inclusion bodies and protein aggregation

7 April 2017

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Human Hsp70 Disaggregase Reverses Parkinson's-Linked α-Synuclein Amyloid Fibrils

7 April 2017

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Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation

28 September 2017

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Type 2 diabetes as a protein misfolding disease.

28 September 2017

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Misfolding, Aggregation, and Disordered Segments in c-Abl and p53 in Human Cancer.

28 September 2017

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Hsp70 forms antiparallel dimers stabilized by post-translational modifications to position clients for transfer to Hsp90.

28 September 2017

1 reference

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Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies

28 September 2017

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Spatially organized aggregation of misfolded proteins as cellular stress defense strategy

28 September 2017

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A functional DnaK dimer is essential for the efficient interaction with Hsp40 heat shock protein

28 September 2017

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Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein

28 September 2017

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Proteostasis impairment in protein-misfolding and -aggregation diseases

28 September 2017

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The amyloid state and its association with protein misfolding diseases.

28 September 2017

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Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy.

28 September 2017

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Suppression of polyglutamine protein toxicity by co-expression of a heat-shock protein 40 and a heat-shock protein 110

28 September 2017

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Protein rescue from aggregates by powerful molecular chaperone machines

28 September 2017

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Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress

28 September 2017

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Regulation of organismal proteostasis by transcellular chaperone signaling

28 September 2017

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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.

28 September 2017

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Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor

28 September 2017

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The nascent polypeptide-associated complex is a key regulator of proteostasis

28 September 2017

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Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm

28 September 2017

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Metazoan Hsp70 machines use Hsp110 to power protein disaggregation

28 September 2017

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DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine

28 September 2017

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Chaperone networks in protein disaggregation and prion propagation

28 September 2017

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Prion-like spread of protein aggregates in neurodegeneration

28 September 2017

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Human heat shock protein 105/110 kDa (Hsp105/110) regulates biogenesis and quality control of misfolded cystic fibrosis transmembrane conductance regulator at multiple levels

28 September 2017

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WormBase 2012: more genomes, more data, new website

28 September 2017

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The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system

28 September 2017

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Characterization of stress sensitivity and chaperone activity of Hsp105 in mammalian cells

28 September 2017

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The stress of protein misfolding: from single cells to multicellular organisms

28 September 2017

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Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling

28 September 2017

1 reference

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Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions

28 September 2017

1 reference

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Cellular strategies for controlling protein aggregation

28 September 2017

1 reference

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Multiple molecules of Hsc70 and a dimer of DjA1 independently bind to an unfolded protein

28 September 2017

1 reference

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Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways

28 September 2017

1 reference

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Hsp104 and ClpB: protein disaggregating machines

28 September 2017

1 reference

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

28 September 2017

1 reference

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Clearance of mutant aggregate-prone proteins by autophagy.

28 September 2017

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The mechanism of Hsp70 chaperones: (entropic) pulling the models together

28 September 2017

1 reference

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Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system

28 September 2017

1 reference

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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.

28 September 2017

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Keep the traffic moving: mechanism of the Hsp70 motor

28 September 2017

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Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling

28 September 2017

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

28 September 2017

1 reference

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Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease.

28 September 2017

1 reference

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

28 September 2017

1 reference

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Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein

28 September 2017

1 reference

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The djlA gene acts synergistically with dnaJ in promoting Escherichia coli growth.

28 September 2017

1 reference

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

28 September 2017

1 reference

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Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress

28 September 2017

1 reference

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

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function

28 September 2017

1 reference

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Leishmania major Hsp100 is required chiefly in the mammalian stage of the parasite

28 September 2017

1 reference

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A novel hsp110-related gene, apg-1, that is abundantly expressed in the testis responds to a low temperature heat shock rather than the traditional elevated temperatures

28 September 2017

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A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

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

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

ClpB is the Escherichia coli heat shock protein F84.1.

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Surface adsorption considerations when working with amyloid fibrils in multiwell plates and Eppendorf tubes

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

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

31 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activity

31 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.

31 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ.

31 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Hsp110 protects heat-denatured proteins and confers cellular thermoresistance.

31 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Thermotolerance in mammalian cells. Protein denaturation and aggregation, and stress proteins.

31 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32

31 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction.

31 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Disruption of ionic interactions between the nucleotide binding domain 1 (NBD1) and middle (M) domain in Hsp100 disaggregase unleashes toxic hyperactivity and partial independence from Hsp70.

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces.

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

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

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

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

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

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

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Human and yeast Hsp110 chaperones exhibit functional differences

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

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

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Substrate recognition by the AAA+ chaperone ClpB.

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104.

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Identification of essential residues in the type II Hsp40 Sis1 that function in polypeptide binding

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Hsp101 is necessary for heat tolerance but dispensable for development and germination in the absence of stress.

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

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

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

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

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Expression of APG-2 protein, a member of the heat shock protein 110 family, in developing rat brain.

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

Identification of a major subfamily of large hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein.

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4598581

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

28 November 2018

1 reference

12 December 2020

The Arabidopsis ClpB/Hsp100 family of proteins: chaperones for stress and chloroplast development

1 reference

12 December 2020

Modulation of the chaperone activities of Hsc70/Hsp40 by Hsp105alpha and Hsp105beta

1 reference

12 December 2020

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

1 reference

12 December 2020

Identifiers

DOI

10.3389/FMOLB.2015.00057

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:26501065%20AND%20SRC:MED&resulttype=core&format=json

28 February 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:26501065%20AND%20SRC:MED&resulttype=core&format=json

28 February 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:26501065%20AND%20SRC:MED&resulttype=core&format=json