Regulated release of ERdj3 from unfolded proteins by BiP (Q24323860)

1

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Walid Awad

2

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Kseniya Petrova

3

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Linda M Hendershot

Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3

4

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language of work or name

English

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publication date

5 November 2008

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published in

The EMBO Journal

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volume

27

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issue

21

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page(s)

2873-82

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cites work

1 reference

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ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates

19 March 2017

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Mechanisms for regulation of Hsp70 function by Hsp40

19 March 2017

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A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins

19 March 2017

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ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress

19 March 2017

1 reference

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Mammalian Sec61 is associated with Sec62 and Sec63

19 March 2017

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The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J-domain of the Escherichia coli DnaJ molecular chaperone

19 March 2017

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Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins

19 March 2017

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

19 March 2017

1 reference

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

19 March 2017

1 reference

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Structural analysis of substrate binding by the molecular chaperone DnaK

19 March 2017

1 reference

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

19 March 2017

1 reference

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Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.

19 March 2017

1 reference

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The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

19 March 2017

1 reference

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Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK

19 March 2017

1 reference

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BiP mutants that are unable to interact with endoplasmic reticulum DnaJ proteins provide insights into interdomain interactions in BiP.

7 April 2017

1 reference

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The role of p58IPK in protecting the stressed endoplasmic reticulum

27 September 2017

1 reference

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Network of general and specialty J protein chaperones of the yeast cytosol

27 September 2017

1 reference

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Structural basis of interdomain communication in the Hsc70 chaperone.

27 September 2017

1 reference

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The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum

27 September 2017

1 reference

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Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

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

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

Purification and properties of BiP.

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

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

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

Initiation of the DNA replication of bacteriophage lambda in Escherichia coli K12

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

Isolation of a mouse cDNA encoding MTJ1, a new murine member of the DnaJ family of proteins

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

Mutations within the nucleotide binding site of immunoglobulin-binding protein inhibit ATPase activity and interfere with release of immunoglobulin heavy chain.

27 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

Different conformations for the same polypeptide bound to chaperones DnaK and GroEL.

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

Structure of the functional fragment of auxilin required for catalytic uncoating of clathrin-coated vesicles.

30 May 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2008.207

Mechanism of the targeting action of DnaJ in the DnaK molecular chaperone system

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2008.207

Swivels and stators in the Hsp40-Hsp70 chaperone machine.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2008.207

The roles of the two zinc binding sites in DnaJ.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2008.207

Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2008.207

Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2008.207

Allosteric regulation of Hsp70 chaperones by a proline switch

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2008.207

Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2008.207

The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2008.207

The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication.

21 January 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2580786

ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates

29 November 2018

1 reference

12 December 2020

In vitro dissociation of BiP-peptide complexes requires a conformational change in BiP after ATP binding but does not require ATP hydrolysis

1 reference

12 December 2020

Cooperative action of Hsp70, Hsp90, and DnaJ proteins in protein renaturation

1 reference

12 December 2020

The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding

1 reference

12 December 2020

The type I Hsp40 zinc finger-like region is required for Hsp70 to capture non-native polypeptides from Ydj1

1 reference

12 December 2020

Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker

1 reference

12 December 2020

Identifiers

DOI

10.1038/EMBOJ.2008.207

1 reference

5002031

5002031

1 reference

1 reference

1 reference