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The COOH-terminal Peptide Binding Domain Is Essential for Self-association of the Molecular Chaperone HSC70

https://doi.org/10.1074/jbc.272.13.8744

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Interconversion of three differentially modified and assembled forms of BiP.

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Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ‐1.

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The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj‐1 have distinct roles in recognition of a non‐native protein and protein refolding.

inferredcites →https://doi.org/10.1002/jcp.1041530215openalex-snapshot

Constitutive HSP70: Oligomerization and its dependence on ATP binding

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Analytical ultracentrifugation in biochemistry and polymer science

inferredcites →https://doi.org/10.1016/0014-5793(79)80427-5openalex-snapshot

Physical Aspects of Protein Interactions

inferredcites →https://doi.org/10.1016/0014-5793(95)90152-3openalex-snapshot

Modern analytical ultracentrifugation. Acquisition and interpretation of data for biological and synthetic polymer systems

inferredcites →https://doi.org/10.1016/0092-8674(95)90099-3openalex-snapshot

Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle

inferredcites →https://doi.org/10.1016/0301-4622(75)80007-xopenalex-snapshot

The direct analysis of sedimentation equilibrium results obtained with polymerizing systems

inferredcites →https://doi.org/10.1016/0301-4622(85)80063-6openalex-snapshot

Determination of the parameters of self-association by direct fitting of the omega function

inferredcites →https://doi.org/10.1016/0959-440x(95)80014-ropenalex-snapshot

Molecular chaperones in cellular protein folding

inferredcites →https://doi.org/10.1016/s0021-9258(17)39211-6openalex-snapshot

ATP catalyzes the sequestration of clathrin during enzymatic uncoating.

inferredcites →https://doi.org/10.1016/s0021-9258(17)42344-1openalex-snapshot

Interaction of 70-kDA heat shock cognate protein with peptides and myo-inositol monophosphatase.

inferredcites →https://doi.org/10.1016/s0021-9258(18)31449-2openalex-snapshot

Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers

inferredcites →https://doi.org/10.1016/s0021-9258(18)43837-9openalex-snapshot

Common and divergent peptide binding specificities of hsp70 molecular chaperones.

inferredcites →https://doi.org/10.1016/s0021-9258(18)52341-3openalex-snapshot

Avian myeloblastosis virus reverse transcriptase. Effect of glycerol on its hydrodynamic properties

inferredcites →https://doi.org/10.1016/s0021-9258(19)52451-6openalex-snapshot

PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT

inferredcites →https://doi.org/10.1016/s0021-9258(19)74274-4openalex-snapshot

Identification of the peptide binding domain of hsc70. 18-Kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding.

inferredcites →https://doi.org/10.1016/s0021-9258(19)75848-7openalex-snapshot

The ATPase core of a clathrin uncoating protein.

inferredcites →https://doi.org/10.1016/s0076-6879(96)66032-7openalex-snapshot

[30] Prediction and analysis of coiled-coil structures

inferredcites →https://doi.org/10.1021/bi00019a001openalex-snapshot

The Peptide-Binding Domain of the Chaperone Protein Hsc70 Has an Unusual Secondary Structure Topology

inferredcites →https://doi.org/10.1021/bi00036a040openalex-snapshot

Kinetics of Nucleotide-Induced Changes in the Tryptophan Fluorescence of the Molecular Chaperone Hsc70 and Its Subfragments Suggest the ATP-Induced Conformational Change Follows Initial ATP Binding

inferredcites →https://doi.org/10.1021/bi00038a002openalex-snapshot

Solution small-angle x-ray scattering study of the molecular chaperone Hsc70 and its subfragments

inferredcites →https://doi.org/10.1021/bi00046a037openalex-snapshot

Self-Association of the Molecular Chaperone HSC70

inferredcites →https://doi.org/10.1021/bi00154a012openalex-snapshot

Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange

inferredcites →https://doi.org/10.1021/bi00359a023openalex-snapshot

Purification and initial characterization of the 71-kilodalton rat heat-shock protein and its cognate as fatty acid binding proteins

inferredcites →https://doi.org/10.1021/bi00843a025openalex-snapshot

Sedimentation equilibrium in reacting systems. VI. Applications to indefinite self-associations. Studies with β-lactoglobulin A

inferredcites →https://doi.org/10.1021/bi951984lopenalex-snapshot

Conformational Characterization of DnaK and Its Complexes by Small-Angle X-ray Scattering

inferredcites →https://doi.org/10.1038/227680a0openalex-snapshot

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

inferredcites →https://doi.org/10.1038/346623a0openalex-snapshot

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

inferredcites →https://doi.org/10.1038/365664a0openalex-snapshot

ATP-induced protein Hsp70 complex dissociation requires K+ but not ATP hydrolysis

inferredcites →https://doi.org/10.1073/pnas.74.12.5463openalex-snapshot

DNA sequencing with chain-terminating inhibitors

inferredcites →https://doi.org/10.1073/pnas.88.13.5719openalex-snapshot

Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding.

inferredcites →https://doi.org/10.1073/pnas.89.6.2081openalex-snapshot

Interactions of liver Grp78 and Escherichia coli recombinant Grp78 with ATP: multiple species and disaggregation.

inferredcites →https://doi.org/10.1074/jbc.270.34.19839openalex-snapshot

Hsc70-binding Peptides Selected from a Phage Display Peptide Library that Resemble Organellar Targeting Sequences

inferredcites →https://doi.org/10.1074/jbc.270.38.22535openalex-snapshot

Polymerization of 70-kDa Heat Shock Protein by Yeast DnaJ in ATP

inferredcites →https://doi.org/10.1074/jbc.270.5.2183openalex-snapshot

The DnaK Chaperone System of Escherichia coli: Quaternary Structures and Interactions of the DnaK and GrpE Components

inferredcites →https://doi.org/10.1074/jbc.270.7.2967openalex-snapshot

Effect of Nucleotide on the Binding of Peptides to 70-kDa Heat Shock Protein

inferredcites →https://doi.org/10.1074/jbc.271.28.16792openalex-snapshot

Effect of Constitutive 70-kDa Heat Shock Protein Polymerization on Its Interaction with Protein Substrate

inferredcites →https://doi.org/10.1074/jbc.271.31.18471openalex-snapshot

Effect of Nucleotides, Peptides, and Unfolded Proteins on the Self-association of the Molecular Chaperone HSC70

inferredcites →https://doi.org/10.1083/jcb.109.4.1457openalex-snapshot

Trimeric binding of the 70-kD uncoating ATPase to the vertices of clathrin triskelia: a candidate intermediate in the vesicle uncoating reaction.

inferredcites →https://doi.org/10.1083/jcb.120.5.1101openalex-snapshot

The constitutive and stress inducible forms of hsp 70 exhibit functional similarities and interact with one another in an ATP-dependent fashion.

inferredcites →https://doi.org/10.1083/jcb.132.3.255openalex-snapshot

Roles of molecular chaperones in protein degradation.

inferredcites →https://doi.org/10.1083/jcb.99.2.723openalex-snapshot

An enzyme that removes clathrin coats: purification of an uncoating ATPase.

inferredcites →https://doi.org/10.1083/jcb.99.2.734openalex-snapshot

Dissociation of clathrin coats coupled to the hydrolysis of ATP: role of an uncoating ATPase.

inferredcites →https://doi.org/10.1104/pp.104.4.1371openalex-snapshot

Differential Influence of ATP on Native Spinach 70-Kilodalton Heat-Shock Cognates

inferredcites →https://doi.org/10.1111/j.1432-1033.1994.00t99.xopenalex-snapshot

Regulation of 70-kDa Heat-Shock-Protein ATPase Activity and Substrate Binding by Human DnaJ-Like Proteins, HSJ1a and HSJ1b

inferredcites →https://doi.org/10.1111/j.1432-1033.1994.tb18720.xopenalex-snapshot

Overexpression in Escherichia coli, purification and characterization of the molecular chaperone HSC70

inferredcites →https://doi.org/10.1126/science.252.5009.1162openalex-snapshot

Predicting Coiled Coils from Protein Sequences

inferredcites →https://doi.org/10.1126/science.271.5255.1519openalex-snapshot

Common Principles of Protein Translocation Across Membranes

inferredcites →https://doi.org/10.1126/science.272.5268.1606openalex-snapshot

Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK

inferredcites →https://doi.org/10.1126/science.2756425openalex-snapshot

Peptide Binding and Release by Proteins Implicated as Catalysts of Protein Assembly

inferredcites →https://doi.org/10.1126/science.7761850openalex-snapshot

Hold 'em and Fold 'em: Chaperones and Signal Transduction

inferredcites →https://doi.org/10.1146/annurev.bi.62.070193.002025openalex-snapshot

MOLECULAR CHAPERONE FUNCTIONS OF HEAT-SHOCK PROTEINS

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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inferred← citeshttps://doi.org/10.1002/mco2.70405openalex-snapshot

cZFP609 Tethering BiP Alleviates Cartilage Degradation in Osteoarthritis via Remedying Aberrant ER‐Mitochondrial Contacts

inferred← citeshttps://doi.org/10.1006/abbi.1999.1354openalex-snapshot

N-Ethylmaleimide-Modified Hsp70 Inhibits Protein Folding

inferred← citeshttps://doi.org/10.1006/bbrc.1999.1321openalex-snapshot

Specificity of Peptide-Induced Depolymerization of the Recombinant Carboxy-Terminal Fragment of BiP/GRP78

inferred← citeshttps://doi.org/10.1006/bbrc.2001.4567openalex-snapshot

A GrpE Mutant Containing the NH2-Terminal “Tail” Region Is Able to Displace Bound Polypeptide Substrate from DnaK

inferred← citeshttps://doi.org/10.1006/prep.2001.1399openalex-snapshot

The Cochaperone Murine Stress-Inducible Protein 1: Overexpression, Purification, and Characterization

inferred← citeshttps://doi.org/10.1007/3-540-29717-0_1openalex-snapshot

Chaperones in Preventing Protein Denaturation in Living Cells and Protecting Against Cellular Stress

inferred← citeshttps://doi.org/10.1007/s12192-011-0307-1openalex-snapshot

Visualization and functional analysis of the oligomeric states of Escherichia coli heat shock protein 70 (Hsp70/DnaK)

inferred← citeshttps://doi.org/10.1007/s12192-014-0526-3openalex-snapshot

C-terminal amino acids are essential for human heat shock protein 70 dimerization

inferred← citeshttps://doi.org/10.1016/j.bbrc.2007.03.107openalex-snapshot

Crystal structure of the C-terminal three-helix bundle subdomain of C. elegans Hsp70

inferred← citeshttps://doi.org/10.1016/j.biocel.2007.10.017openalex-snapshot

The Agrobacterium tumefaciens DnaK: ATPase cycle, oligomeric state and chaperone properties

inferred← citeshttps://doi.org/10.1016/j.febslet.2004.09.044openalex-snapshot

Role of the C‐terminal region of mouse inducible Hsp72 in the recognition of peptide substrate for chaperone activity

inferred← citeshttps://doi.org/10.1016/j.heliyon.2024.e29690openalex-snapshot

Swapping the linkers of canonical Hsp70 and Hsp110 chaperones compromises both self-association and client selection

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2018.11.130openalex-snapshot

Studies on the effect of the J-domain on the substrate binding domain (SBD) of Hsp70 using a chimeric human J-SBD polypeptide

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The effect of the hexahistidine-tag in the oligomerization of HSC70 constructs

inferred← citeshttps://doi.org/10.1016/j.jprot.2014.02.004openalex-snapshot

Structural and functional characterization of the chaperone Hsp70 from sugarcane. Insights into conformational changes during cycling from cross-linking/mass spectrometry assays

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Overproduction, purification, and characterization of the Plasmodium falciparum heat shock protein 70

inferred← citeshttps://doi.org/10.1016/s0161-5890(99)00136-4openalex-snapshot

Immunostimulatory properties of the Leishmania infantum heat shock proteins HSP70 and HSP83

inferred← citeshttps://doi.org/10.1021/a1980015topenalex-snapshot

Size Exclusion Chromatography and Related Separation Techniques

inferred← citeshttps://doi.org/10.1021/acs.jproteome.6c00037openalex-snapshot

Novel Insights into the Human Hsc70 Structure by Cross-Linking Mass Spectrometry and Molecular Modeling

inferred← citeshttps://doi.org/10.1021/bi100386wopenalex-snapshot

Balance between Folding and Degradation for Hsp90-Dependent Client Proteins: A Key Role for CHIP

inferred← citeshttps://doi.org/10.1021/bi980597jopenalex-snapshot

Conformational Changes of an Hsp70 Molecular Chaperone Induced by Nucleotides, Polypeptides, and N-Ethylmaleimide

inferred← citeshttps://doi.org/10.1023/b:dobs.0000025249.83552.ddopenalex-snapshot

LAK Cells Kill Fas– Cancer Cells Using the Tag7/Hsp70 Protein Complex Secreted from the Golgi Apparatus

inferred← citeshttps://doi.org/10.1023/b:dobs.0000025250.13498.88openalex-snapshot

HSP70 Forms a Stable Cytotoxic Complex with Tag7/PGRP-S

inferred← citeshttps://doi.org/10.1034/j.1399-3054.2001.1130402.xopenalex-snapshot

Plant Hsp70 molecular chaperones: Protein structure, gene family, expression and function

inferred← citeshttps://doi.org/10.1038/ncomms6484openalex-snapshot

Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop

inferred← citeshttps://doi.org/10.1038/s41598-018-34887-6openalex-snapshot

Blocking nuclear export of HSPA8 after heat shock stress severely alters cell survival

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A new look at Hsp70 activity in phosphatidylserine-enriched membranes: chaperone-induced quasi-interdigitated lipid phase

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Oligomerization of the 17‐kDa peptide‐binding domain of the molecular chaperone HSC70

inferred← citeshttps://doi.org/10.1046/j.1432-1327.1999.00078.xopenalex-snapshot

Aggregation of hsp70 and hsc70 in vivo is distinct and temperature‐dependent and their chaperone function is directly related to non‐aggregated forms

inferred← citeshttps://doi.org/10.1073/pnas.95.11.6108openalex-snapshot

Role of the J-domain in the cooperation of Hsp40 with Hsp70

inferred← citeshttps://doi.org/10.1074/jbc.272.40.24825openalex-snapshot

A Mutational Study of the Peptide-binding Domain of Hsc70 Guided by Secondary Structure Prediction

inferred← citeshttps://doi.org/10.1074/jbc.273.35.22506openalex-snapshot

Characterization of Interactions between the Anti-apoptotic Protein BAG-1 and Hsc70 Molecular Chaperones

inferred← citeshttps://doi.org/10.1074/jbc.273.41.26827openalex-snapshot

Substrate Binding Induces Depolymerization of the C-terminal Peptide Binding Domain of Murine GRP78/BiP

inferred← citeshttps://doi.org/10.1074/jbc.m005226200openalex-snapshot

ATP and ADP Modulate a Cation Channel Formed by Hsc70 in Acidic Phospholipid Membranes

inferred← citeshttps://doi.org/10.1074/jbc.m103773200openalex-snapshot

Stoichiometry, Abundance, and Functional Significance of the hsp90/hsp70-based Multiprotein Chaperone Machinery in Reticulocyte Lysate

inferred← citeshttps://doi.org/10.1074/jbc.m106881200openalex-snapshot

Domain Structure of the HSC70 Cochaperone, HIP

inferred← citeshttps://doi.org/10.1074/jbc.m304469200openalex-snapshot

Visualization and Mechanism of Assembly of a Glucocorticoid Receptor·Hsp70 Complex That Is Primed for Subsequent Hsp90-dependent Opening of the Steroid Binding Cleft

inferred← citeshttps://doi.org/10.1074/jbc.m304563200openalex-snapshot

Crystal Structure of the C-terminal 10-kDa Subdomain of Hsc70

inferred← citeshttps://doi.org/10.1074/jbc.m307513200openalex-snapshot

Peptidoglycan Recognition Protein Tag7 Forms a Cytotoxic Complex with Heat Shock Protein 70 in Solution and in Lymphocytes

inferred← citeshttps://doi.org/10.1089/rej.2014.1620openalex-snapshot

Anti-Inflammatory Peptide Regulates the Supply of Heat Shock Protein 70 Monomers: Implications for Aging and Age-Related Disease

inferred← citeshttps://doi.org/10.1093/jb/mvj071openalex-snapshot

A Disulfide Bridge Mediated by Cysteine 574 Is Formed in the Dimer of the 70-kDa Heat Shock Protein

inferred← citeshttps://doi.org/10.1096/fj.04-2088comopenalex-snapshot

Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability

inferred← citeshttps://doi.org/10.1098/rstb.2016.0526openalex-snapshot

Membrane heat shock protein 70: a theranostic target for cancer therapy

inferred← citeshttps://doi.org/10.1107/s1744309106032064openalex-snapshot

Crystallization and X-ray data analysis of the 10 kDa C-terminal lid subdomain fromCaenorhabditis elegansHsp70

inferred← citeshttps://doi.org/10.1128/jb.01131-08openalex-snapshot

Allosteric Coupling between the Lid and Interdomain Linker in DnaK Revealed by Inhibitor Binding Studies

inferred← citeshttps://doi.org/10.1128/mcb.19.6.4535openalex-snapshot

Identification of CHIP, a Novel Tetratricopeptide Repeat-Containing Protein That Interacts with Heat Shock Proteins and Negatively Regulates Chaperone Functions

inferred← citeshttps://doi.org/10.1134/s0006297913050118openalex-snapshot

Hsp70 from Cyprinion macrostomus macrostomus and Garra rufa obtuse: Stability and stability-dependent activity

inferred← citeshttps://doi.org/10.12688/f1000research.15528.1openalex-snapshot

Hsp70 chaperone: a master player in protein homeostasis

inferred← citeshttps://doi.org/10.1371/journal.pcbi.1004262openalex-snapshot

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

inferred← citeshttps://doi.org/10.1371/journal.pone.0067961openalex-snapshot

Hsp70 Oligomerization Is Mediated by an Interaction between the Interdomain Linker and the Substrate-Binding Domain

inferred← citeshttps://doi.org/10.1379/csc-26r.1openalex-snapshot

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

inferred← citeshttps://doi.org/10.3389/fmolb.2019.00081openalex-snapshot

Oligomerization of Hsp70: Current Perspectives on Regulation and Function

inferred← citeshttps://doi.org/10.3390/biom10060856openalex-snapshot

Comparative Characterization of Plasmodium falciparum Hsp70-1 Relative to E. coli DnaK Reveals the Functional Specificity of the Parasite Chaperone

inferred← citeshttps://doi.org/10.3390/biom9100543openalex-snapshot

The Link That Binds: The Linker of Hsp70 as a Helm of the Protein’s Function

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