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Quality control and fate determination of Hsp90 client proteins
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scholarly article
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PubMed
review article
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title
Quality control and fate determination of Hsp90 client proteins
(English)
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PubMed
main subject
cell biology
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quality control
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author name string
Maria A. Theodoraki
series ordinal
1
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Crossref
Avrom J. Caplan
series ordinal
2
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stated in
Crossref
language of work or name
English
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stated in
PubMed
publication date
March 2012
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stated in
PubMed
published in
Biochimica et Biophysica Acta
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PubMed
volume
1823
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stated in
PubMed
issue
3
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PubMed
page(s)
683-8
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PubMed
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Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis
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The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system
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The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
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The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
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Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
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p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function
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Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
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Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation
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Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins
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Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1
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Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturation
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Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein
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Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
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ErbB2 degradation mediated by the co-chaperone protein CHIP
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C-terminal Hsp-interacting protein slows androgen receptor synthesis and reduces its rate of degradation
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CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation
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Targeting the dynamic HSP90 complex in cancer
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Hsp90 as a capacitor for morphological evolution
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The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent
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HSP90 at the hub of protein homeostasis: emerging mechanistic insights
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Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
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The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
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Protein quality control at the plasma membrane
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Exposed hydrophobicity is a key determinant of nuclear quality control degradation
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Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone
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Hsp90 and environmental stress transform the adaptive value of natural genetic variation
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Quality control for unfolded proteins at the plasma membrane
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Balance between folding and degradation for Hsp90-dependent client proteins: a key role for CHIP.
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Peripheral protein quality control removes unfolded CFTR from the plasma membrane
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Heat shock protein 90 in neurodegenerative diseases
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Chaperone-assisted degradation: multiple paths to destruction
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Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system
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Regulation of Hsp90 client proteins by a Cullin5-RING E3 ubiquitin ligase
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Intranuclear degradation of polyglutamine aggregates by the ubiquitin-proteasome system.
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CHIP deletion reveals functional redundancy of E3 ligases in promoting degradation of both signaling proteins and expanded glutamine proteins
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28 September 2017
Ydj1 protects nascent protein kinases from degradation and controls the rate of their maturation.
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28 September 2017
The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2.
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28 September 2017
Silencing of HSP90 cochaperone AHA1 expression decreases client protein activation and increases cellular sensitivity to the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin
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28 September 2017
Selective compounds define Hsp90 as a major inhibitor of apoptosis in small-cell lung cancer
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28 September 2017
Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies
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28 September 2017
All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.
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The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies
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Protein misassembly: macromolecular crowding and molecular chaperones
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28 September 2017
Molecular chaperones and protein kinase quality control.
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28 September 2017
Structure of an Hsp90-Cdc37-Cdk4 complex.
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28 September 2017
V600E B-Raf requires the Hsp90 chaperone for stability and is degraded in response to Hsp90 inhibitors
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28 September 2017
17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration
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28 September 2017
The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation
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28 September 2017
Hsp90 and Cdc37 -- a chaperone cancer conspiracy.
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Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex.
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28 September 2017
Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase
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The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability
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28 September 2017
Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu
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28 September 2017
The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome
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28 September 2017
Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils
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28 September 2017
Posttranslational quality control: folding, refolding, and degrading proteins.
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28 September 2017
Differential effects of the hsp70-binding protein BAG-1 on glucocorticoid receptor folding by the hsp90-based chaperone machinery
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28 September 2017
Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function
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28 September 2017
Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae
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28 September 2017
p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2.
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28 September 2017
Heat-shock protein hsp90 governs the activity of pp60v-src kinase
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28 September 2017
Substrate-binding sites of UBR1, the ubiquitin ligase of the N-end rule pathway
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31 May 2018
Cytoplasmic Hsp70 promotes ubiquitination for endoplasmic reticulum-associated degradation of a misfolded mutant of the yeast plasma membrane ATPase, PMA1.
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31 May 2018
CHIP (carboxyl terminus of Hsc70-interacting protein) promotes basal and geldanamycin-induced degradation of estrogen receptor-alpha
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31 May 2018
CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
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31 May 2018
Involvement of heat shock protein 90 in the degradation of mutant insulin receptors by the proteasome.
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31 May 2018
Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells
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31 May 2018
Heat Shock Protein 70 Inhibits α-Synuclein Fibril Formation via Interactions with Diverse Intermediates
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3242914
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28 November 2018
Heat shock proteins 70 and 90 inhibit early stages of amyloid beta-(1-42) aggregation in vitro.
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3242914
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28 November 2018
Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology
1 reference
stated in
PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3242914
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28 November 2018
Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3242914
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28 November 2018
Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70.
1 reference
stated in
PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3242914
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28 November 2018
Post-translational disruption of the delta F508 cystic fibrosis transmembrane conductance regulator (CFTR)-molecular chaperone complex with geldanamycin stabilizes delta F508 CFTR in the rabbit reticulocyte lysate.
1 reference
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PubMed Central
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28 November 2018
Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein
1 reference
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PubMed
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
CYP2E1 degradation by in vitro reconstituted systems: role of the molecular chaperone hsp90
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/21871502
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/21871502
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Depletion of the erbB-2 gene product p185 by benzoquinoid ansamycins
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/21871502
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1016/J.BBAMCR.2011.08.006
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3151504
OpenCitations bibliographic resource ID
3151504
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3151504
PMC publication ID
3242914
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3151504
PubMed publication ID
21871502
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3151504
ResearchGate publication ID
51599552
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