Interaction of the Chaperone BiP with an Antibody Domain: Implications for the Chaperone Cycle

Knarr, Gerhard; Kies, Ursula; Bell, Stefan; Mayer, Marcus; Büchner, Johannes

doi:10.1016/s0022-2836(02)00166-3

Cited by 14 publications

(12 citation statements)

References 49 publications

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“…28 It has been shown previously that C H 3-CAM forms stable binary complexes with BiP. 28 Here, we have analyzed the individual steps of the ATPase cycle of BiP. We show how a polypeptide substrate and a short peptide, respectively, modulate the ATPase cycle.…”

Section: Introductionmentioning

confidence: 89%

“…To address this question, we formed complexes of BiP and C H 3-CAM as described previously. 28 When we measured the ATPase activity of the BiP·C H 3-CAM complex by steady state (Figure 3(A)) and single turnover experiments (Figure 3(B)), surprisingly both showed a decrease To test whether this effect can be reversed by the addition of peptide, we added HD14 to a preformed BiP·C H 3-CAM complex and monitored the effect on the ATPase activity of BiP. In the presence of an excess of peptide HD14 we observed an increase in the ATPase activity of BiP (Figure 3(C)).…”

Section: Complex Formation With C H 3-cam Decelerates the Atpase Actimentioning

confidence: 99%

“…The C H 3-CAM domain is a non-native, but soluble polypeptide. 28 It has been shown previously that C H 3-CAM forms stable binary complexes with BiP. 28 Here, we have analyzed the individual steps of the ATPase cycle of BiP.…”

Section: Introductionmentioning

confidence: 99%

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Modulation of the ATPase Cycle of BiP by Peptides and Proteins

Mayer

Reinstein

Büchner

2003

Journal of Molecular Biology

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Section: Introductionmentioning

confidence: 89%

Section: Complex Formation With C H 3-cam Decelerates the Atpase Actimentioning

confidence: 99%

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Modulation of the ATPase Cycle of BiP by Peptides and Proteins

Mayer

Reinstein

Büchner

2003

Journal of Molecular Biology

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“…Titrations of different combinations of fragments revealed that the affinity is determined by the interaction of Hsp90 with the DBD of p53. The binding constant of ϳ1 M is in the range of substrate binding to Hsp70 (68). Interestingly, the middle domain and to some extent also the carboxy-terminal domain of Hsp90 are sufficient to protect p53 from thermal unfolding.…”

Section: Figmentioning

confidence: 99%

Hsp90 Regulates the Activity of Wild Type p53 under Physiological and Elevated Temperatures

Müller

Schaupp

Walerych

et al. 2004

Journal of Biological Chemistry

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134

111

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The activity and structural integrity of the tumor suppressor protein p53 is of crucial importance for the prevention of cancer. p53 is a conformational flexible and labile protein, in which structured and unstructured regions function in a synergistic manner. The molecular chaperone Hsp90 is known to bind to mutant and wild type p53 in vivo. Using highly purified proteins we analyzed the interaction and the binding sites between both proteins in detail. Our results demonstrate that Hsp90 binds to a folded, native-like conformation of p53 in vitro with micromolar affinity. Specifically, the DNAbinding domain of p53 and the middle and carboxyterminal domains of Hsp90 are responsible for this interaction, which is essential to stabilize p53 at physiological temperatures and to prevent it from irreversible thermal inactivation. Our results are in agreement with a model in which Hsp90 is required to maintain the folded, active state of p53 by a reversible interaction, thus introducing an additional level of regulation.

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“…Dimerization mimics the interactions of Hsp70 proteins with target polypeptides and denatured proteins in many regards. It can be reversed by the addition of short peptides (suggesting competition for the same peptide binding site) or by addition of ATP (Benaroudj et al 1995;Blond-Elguindi et al 1993b;Knarr et al 2002). The region of Hsp70 proteins responsible for intermolecular association is not known with certainty.…”

Section: Structural and Functional Properties Of Hsp70mentioning

confidence: 99%

Hsp70 and Hsp90—a relay team for protein folding

Wegele

Müller

Büchner

Reviews of Physiology, Biochemistry and Pharmacology

567

492

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Molecular chaperones are a functionally defined set of proteins which assist the structure formation of proteins in vivo. Without certain protective mechanisms, such as binding nascent polypeptide chains by molecular chaperones, cellular protein concentrations would lead to misfolding and aggregation. In the mammalian system, the molecular chaperones Hsp70 and Hsp90 are involved in the folding and maturation of key regulatory proteins, like steroid hormone receptors, transcription factors, and kinases, some of which are involved in cancer progression. Hsp70 and Hsp90 form a multichaperone complex, in which both are connected by a third protein called Hop. The connection of and the interplay between the two chaperone machineries is of crucial importance for cell viability. This review provides a detailed view of the Hsp70 and Hsp90 machineries, their cofactors and their mode of regulation. It summarizes the current knowledge in the field, including the ATP-dependent regulation of the Hsp70/Hsp90 multichaperone cycle and elucidates the complex interplay and their synergistic interaction.

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Interaction of the Chaperone BiP with an Antibody Domain: Implications for the Chaperone Cycle

Cited by 14 publications

References 49 publications

Modulation of the ATPase Cycle of BiP by Peptides and Proteins

Modulation of the ATPase Cycle of BiP by Peptides and Proteins

Hsp90 Regulates the Activity of Wild Type p53 under Physiological and Elevated Temperatures

Hsp70 and Hsp90—a relay team for protein folding

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