Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker.

No abstract is available for this paper.

• Publication year

  2007

• Venue

  Molecules and Cells

• Publication date

  2007-04-13

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/J.MOLCEL.2007.02.020PMID 17434124PMCID PMC1894942
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Ionic Contacts at DnaK Substrate Binding Domain Involved in the Allosteric Regulation of Lid Dynamics*

  2006cited by this paper
• Amide Hydrogen Exchange Reveals Conformational Changes in Hsp70 Chaperones Important for Allosteric Regulation*

  2006influential reference
• Molecular chaperones and protein quality control.

  2006cited by this paper
• The allosteric transition in DnaK probed by infrared difference spectroscopy. Concerted ATP‐induced rearrangement of the substrate binding domain

  2006cited by this paper
• The changing landscape of protein allostery.

  2006cited by this paper
• Allosteric Regulation of Hsp70 Chaperones Involves a Conserved Interdomain Linker*

  2006influential reference
• Direct Comparison of a Stable Isolated Hsp70 Substrate-binding Domain in the Empty and Substrate-bound States*

  2006influential reference
• Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly.

  2005cited by this paper
• Hsp70 chaperones: Cellular functions and molecular mechanism

  2005influential reference
• Structural basis of interdomain communication in the Hsc70 chaperone.

  2005influential reference
• NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70 molecular chaperone.

  2005influential reference
• Pathways of chaperone-mediated protein folding in the cytosol

  2004cited by this paper
• Understanding the allosteric mechanism of the Escherichia coli Hsp70 molecular chaperone, DnaK

  2004cited by this paper
• Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase.

  2004cited by this paper
• Actin-binding proteins--a unifying hypothesis.

  2004cited by this paper
• Interdomain interaction through helices A and B of DnaK peptide binding domain

  2003influential reference
• Detection of a concerted conformational change in the ATPase domain of DnaK triggered by peptide binding

  2003cited by this paper
• Characterization of two partially unfolded intermediates of the molecular chaperone DnaK at low pH.

  2002cited by this paper
• Studies of biomolecular conformations and conformational dynamics by mass spectrometry.

  2002cited by this paper
• Structure of a Bag/Hsc70 Complex: Convergent Functional Evolution of Hsp70 Nucleotide Exchange Factors

  2001cited by this paper
• Mutations in the interdomain linker region of DnaK abolish the chaperone action of the DnaK/DnaJ/GrpE system

  2001cited by this paper
• Structural insights into substrate binding by the molecular chaperone DnaK

  2000cited by this paper
• Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy.

  1999cited by this paper
• Structural analyses of CREB-CBP transcriptional activator-coactivator complexes by NMR spectroscopy: implications for mapping the boundaries of structural domains.

  1999influential reference
• Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling.

  1999influential reference
• Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones.

  1999influential reference
• Peptide-induced conformational changes in the molecular chaperone DnaK.

  1998cited by this paper
• Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK.

  1997cited by this paper
• The second step of ATP binding to DnaK induces peptide release.

  1996cited by this paper
• Three-dimensional structure of ectatomin from Ectatomma tuberculatum ant venom

  1995cited by this paper
• Solution small-angle X-ray scattering study of the molecular chaperone Hsc70 and its subfragments.

  1995influential reference
• Modulation of the ATPase Activity of the Molecular Chaperone DnaK by Peptides and the DnaJ and GrpE Heat Shock Proteins (*)

  1995cited by this paper
• Nucleotide-induced Conformational Changes in the ATPase and Substrate Binding Domains of the DnaK Chaperone Provide Evidence for Interdomain Communication (*)

  1995influential reference
• The program XEASY for computer-supported NMR spectral analysis of biological macromolecules

  1995cited by this paper
• Structural Basis of the 'IO-Kilodalton Heat Shock Cognate Protein ATP Hydrolytic Activity

  1994cited by this paper
• Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment.

  1994cited by this paper
• ATP-induced protein Hsp70 complex dissociation requires K+ but not ATP hydrolysis

  1993cited by this paper
• DnaK, hsp73, and their molten globules. Two different ways heat shock proteins respond to heat.

  1992influential reference
• Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

  1990cited by this paper
• Probing conformational changes in proteins by mass spectrometry

  1990cited by this paper
• NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteriation.

  1988cited by this paper

• Aedes aegypti Hsp70 has enhanced ATPase and protein protection under oxidative stress.

  2026cites this paper
• The nucleotide exchange factor, GrpE, modulates substrate affinity by interaction of its N-terminal tails with the DnaK substrate-binding domain.

  2026cites this paper
• The nucleotide exchange factor, GrpE, modulates substrate affinity by interaction of its N-terminal tails with the DnaK substrate-binding domain

  2025cites this paper
• Unraveling the Molecular Inhibition and Conformational Changes of Hsp70 and Hsc70 Induced by VER-155008, a Competitive ATPase Inhibitor through Molecular Dynamics Simulations and Principal Component Analysis

  2025cites this paper
• A dynamic structural framework for the allosteric regulation of Hsp70 chaperones

  2025cites this paper
• From Rat Tails to Glycoproteostasis: Motivated by Biology, Enabled by Biophysics, and Lucky.

  2025cites this paper
• Membrane-tethered SCOTIN condensates elicit an endoplasmic reticulum stress response by sequestering luminal BiP.

  2025cites this paper
• Hsp110 nucleotide exchange factors may amplify Hsp70-disaggregation by enhanced entropic pulling

  2025cites this paper
• Malate initiates a proton-sensing pathway essential for pH regulation of inflammation

  2024cites this paper
• The ATPase activity of yeast chromosome axis protein Hop1 affects the frequency of meiotic crossovers

  2024cites this paper
• Cleavage of Hsp70.1 causes lysosomal cell death under stress conditions

  2024cites this paper
• Molecular dynamics simulations shows real-time lid opening in Hsp70 chaperone.

  2024cites this paper
• Structure of the M. tuberculosis DnaK−GrpE complex reveals how key DnaK roles are controlled

  2024cites this paper
• Towards the understanding of molecular motors and its relationship with local unfolding

  2024cites this paper
• Conformational plasticity of a BiP–GRP94 chaperone complex

  2024cites this paper
• New insights into the structure and function of the complex between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE

  2023influential citation
• Hsp Inhibitor is Affective Against Adenocarcinomic Human Alveolar Basal Epithelial Cells Through Modulating ERK/MAPK Signaling Pathway

  2023cites this paper
• Nucleotide Exchange Factors for Hsp70 Molecular Chaperones: GrpE, Hsp110/Grp170, HspBP1/Sil1, and BAG Domain Proteins.

  2023cites this paper
• The multifunction of HSP70 in cancer: Guardian or traitor to the survival of tumor cells and the next potential therapeutic target.

  2023cites this paper
• Molecular dynamics simulations suggest novel allosteric modes in the Hsp70 chaperone protein

  2023cites this paper
• Molecular mechanisms of chaperone‐directed protein folding: Insights from atomistic simulations

  2023cites this paper
• Heat Shock Proteins in Non-Small-Cell Lung Cancer-Functional Mechanism.

  2023cites this paper
• Protein folding in vitro and in the cell: From a solitary journey to a team effort.

  2022cites this paper
• Direct observation of chemo-mechanical coupling in the Hsp70 chaperone DnaK by single-molecule force experiments.

  2022cites this paper
• Conformational dynamics of the Hsp70 chaperone throughout key steps of its ATPase cycle

  2022cites this paper
• Two distinct classes of cochaperones compete for the EEVD motif in heat shock protein 70 to tune its chaperone activities

  2022influential citation
• Novel function of the C-Terminal region of the Hsp110 family member Osp94 in unfolded protein refolding.

  2022cites this paper
• General Structural and Functional Features of Molecular Chaperones.

  2021cites this paper
• Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system

  2021cites this paper
• Fic and non-Fic AMPylases: protein AMPylation in metazoans

  2021cites this paper
• The functions and regulation of heat shock proteins; key orchestrators of proteostasis and the heat shock response

  2021cites this paper
• Structural Communication between the E. coli Chaperones DnaK and Hsp90

  2021cites this paper
• A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins

  2021cites this paper
• Interdomain interactions dictate the function of the Candida albicans Hsp110 protein Msi3

  2021cites this paper
• The Hsp70-Chaperone Machines in Bacteria

  2021cites this paper
• Cytosolic protein quality control machinery: Interactions of Hsp70 with a network of co-chaperones and substrates

  2021influential citation
• Characterisation of a unique linker segment of the Plasmodium falciparum cytosol localised Hsp110 chaperone.

  2021cites this paper
• Conformational dynamics of free and membrane-bound human Hsp70 in model cytosolic and endo-lysosomal environments

  2021cites this paper
• Conformational equilibria in allosteric control of Hsp70 chaperones.

  2021cites this paper
• Two distinct classes of co-chaperones compete for the EEVD motif in heat shock protein 70 (Hsp70) to tune its activity

  2021cites this paper
• Redefining Molecular Chaperones as Chaotropes

  2021cites this paper
• Inhibition of the Human Hsc70 System by Small Ligands as a Potential Anticancer Approach

  2021cites this paper
• The Multifaceted Role of HSF1 in Pathophysiology: Focus on Its Interplay with TG2

  2021cites this paper
• Comparative analysis of the coordinated motion of Hsp70s from different organelles observed by single-molecule three-color FRET

  2021influential citation
• A novel and unique ATP hydrolysis to AMP by a human Hsp70 Binding immunoglobin protein (BiP)

  2021influential citation
• Repurposing p97 inhibitors for chemical modulation of the bacterial ClpB–DnaK bichaperone system

  2020cites this paper
• Theory of Allosteric Regulation in Hsp70 Molecular Chaperones

  2020cites this paper
• Structural and functional analysis of the Hsp70/Hsp40 chaperone system

  2020cites this paper
• GR chaperone cycle mechanism revealed by cryo-EM: inactivation of GR by GR:Hsp90:Hsp70:Hop client-loading complex

  2020cites this paper
• Tryptophan scanning mutagenesis as a way to mimic the compound-bound state and probe the selectivity of allosteric inhibitors in cells†

  2020cites this paper
• Two-step mechanism of J-domain action in driving Hsp70 function

  2020cites this paper
• Structure of the substrate-binding domain of Plasmodium falciparum heat-shock protein 70-x

  2020cites this paper
• Hsp70-mediated quality control: should I stay or should I go?

  2020cites this paper
• Dynamic View of Allosteric Regulation in the Hsp70 Chaperones by J-Domain Cochaperone and Post-Translational Modifications: Computational Analysis of Hsp70 Mechanisms by Exploring Conformational Landscapes and Residue Interaction Networks

  2020cites this paper
• Structural influence of the conserved Hsp40 HPD tripeptide on Hsp70 chaperone function

  2020influential citation
• Co-Chaperones in Targeting and Delivery of Misfolded Proteins to the 26S Proteasome

  2020influential citation
• Hsp70 in cancer: A double agent in the battle between survival and death

  2020cites this paper
• Insights from the molecular docking analysis of phytohormone reveal brassinolide interaction with HSC70 from Pennisetum glaucum

  2019cites this paper
• Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines.

  2019cites this paper
• The Complex Phosphorylation Patterns That Regulate the Activity of Hsp70 and Its Cochaperones

  2019cites this paper
• Discorhabdin N, a South African Natural Compound, for Hsp72 and Hsc70 Allosteric Modulation: Combined Study of Molecular Modeling and Dynamic Residue Network Analysis

  2019cites this paper
• An unexpected second binding site for polypeptide substrates is essential for Hsp70 chaperone activity

  2019cites this paper
• Identifying coupled clusters of allostery participants through chemical shift perturbations

  2019cites this paper
• Understanding mechanistic regulation of Hsp70 and Hsp90 in neurodegenerative diseases.

  2019cites this paper
• A History of Molecular Chaperone Structures in the Protein Data Bank

  2019influential citation
• The Link That Binds: The Linker of Hsp70 as a Helm of the Protein’s Function

  2019cites this paper
• Functional principles and regulation of molecular chaperones.

  2019cites this paper
• HSPA1A conformational mutants reveal a conserved structural unit in Hsp70 proteins.

  2019cites this paper
• Analysis of Protein-Protein Interaction in a Single Live Cell by Using a FRET System Based on Genetic Code Expansion Technology.

  2019cites this paper
• Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate

  2018cites this paper
• Glucose-regulated protein 78 substrate-binding domain alters its conformation upon EGCG inhibitor binding to nucleotide-binding domain: Molecular dynamics studies

  2018cites this paper
• Mechanical properties of BiP protein determined by nano‐rheology

  2018cites this paper
• Raman and Infrared Spectra of Acoustical, Functional Modes of Proteins from All-Atom and Coarse-Grained Normal Mode Analysis

  2018cites this paper
• Hsp70: A Multi-Tasking Chaperone at the Crossroad of Cellular Proteostasis

  2018cites this paper
• Disrupted Hydrogen-Bond Network and Impaired ATPase Activity in an Hsc70 Cysteine Mutant.

  2018cites this paper
• Aptamers: Uptake mechanisms and intracellular applications

  2018cites this paper
• Exploration of Benzothiazole Rhodacyanines as Allosteric Inhibitors of Protein-Protein Interactions with Heat Shock Protein 70 (Hsp70).

  2018cites this paper
• Histone methyltransferase KMT5A gene modulates oncogenesis and lipid metabolism of papillary thyroid cancer in vitro.

  2018cites this paper
• The nucleotide-bound/substrate-bound conformation of the Mycoplasma genitalium DnaK chaperone.

  2018cites this paper
• Substrate Binding Switches the Conformation at the Lynchpin Site in the Substrate-Binding Domain of Human Hsp70 to Enable Allosteric Interdomain Communication

  2018cites this paper
• Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions

  2018cites this paper
• Mechanical Properties of Chaperone BiP, the Master Regulator of the Endoplasmic Reticulum

  2018cites this paper
• Human Stress-inducible Hsp70 Has a High Propensity to Form ATP-dependent Antiparallel Dimers That Are Differentially Regulated by Cochaperone Binding*

  2018cites this paper
• Dynamics of a Protein Chain Motor Driving Helical Bacteria under Stress.

  2018cites this paper
• 3 Abbreviations NBD , Nucleotide Binding Domain SBD , Substrate Binding Domain PMF , Peptide Mass Fingerprinting

  2018cites this paper
• Subcellular Hsp70 Inhibitors Promote Cancer Cell Death via Different Mechanisms.

  2018cites this paper
• Intra-molecular pathways of allosteric control in Hsp70s

  2018cites this paper
• Allosteric Modulators of HSP90 and HSP70: Dynamics Meets Function through Structure-Based Drug Design.

  2018cites this paper
• The nucleotide‐bound/substrate‐bound conformation of the Mycoplasma genitalium DnaK chaperone

  2018cites this paper
• Allosteric landscapes of eukaryotic cytoplasmic Hsp70s are shaped by evolutionary tuning of key interfaces

  2018cites this paper
• Sequence-to-Conformation Relationships of Disordered Regions Tethered to Folded Domains of Proteins.

  2018cites this paper
• Regulation of mammalian IRE1α : co-chaperones and their importance

  2018cites this paper
• Investigating energy‐based pool structure selection in the structure ensemble modeling with experimental distance constraints: The example from a multidomain protein Pub1

  2018cites this paper
• Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones

  2018cites this paper
• Fluorescent-Linked Enzyme Chemoproteomic Strategy (FLECS) for Identifying HSP70 Inhibitors.

  2018cites this paper
• The remarkable multivalency of the Hsp70 chaperones

  2017cites this paper
• ISTANBUL TECHNICAL UNIVERSITY GRADUATE SCHOOL OF SCIENCE ENGINEERING AND TECHNOLOGY MOLECULAR DYNAMICS SIMULATION ANALYSIS OF HIS226 MUTATION ON THE DYNAMICS OF THE ATPASE DOMAIN OF DNAK M.Sc. THESIS

  2017influential citation
• The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases

  2017cites this paper
• Allosteric fine-tuning of the conformational equilibrium poises the chaperone BiP for post-translational regulation

  2017influential citation
• Implication du chaperome de la protéine F508del-CFTR dans son transport intracellulaire et/ou sa dégradation : rôle des lectines EDEMs et de la mannosidase du RE

  2017cites this paper