Status: Bibliographieeintrag
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| Verfasst von: | Boysen, Marta [VerfasserIn]  |
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| | Kityk, Roman [VerfasserIn] |
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| | Mayer, Matthias P. [VerfasserIn] |
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| Titel: | Hsp70- and Hsp90-mediated regulation of the conformation of p53 DNA binding domain and p53 cancer variants |
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| Verf.angabe: | Marta Boysen, Roman Kityk, and Matthias P. Mayer |
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| E-Jahr: | 2019 |
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| Jahr: | 23 April 2019 |
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| Umfang: | 17 S. |
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| Fussnoten: | The article ends with page 843.e4 ; Gesehen am 26.06.2019 |
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| Titel Quelle: | Enthalten in: Molecular cell |
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| Ort Quelle: | [Cambridge, Mass.] : Cell Press, 1997 |
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| Jahr Quelle: | 2019 |
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| Band/Heft Quelle: | 74(2019), 4, Seite 831-843 |
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| ISSN Quelle: | 1097-4164 |
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| Abstract: | Summary - The activity of the tumor suppressor p53 has to be timed and balanced closely to prevent untimely induction of cell death. The stability of p53 depends on the ubiquitin ligase Mdm2 but also on Hsp70 and Hsp90 chaperones that interact with its DNA binding domain (DBD). Using hydrogen exchange mass spectrometry and biochemical methods, we analyzed conformational states of wild-type p53-DBD at physiological temperatures and conformational perturbations in three frequent p53 cancer mutants. We demonstrate that the Hsp70/Hdj1 system shifts the conformational equilibrium of p53 toward a flexible, more mutant-like, DNA binding inactive state by binding to the DNA binding loop. The analyzed cancer mutants are likewise destabilized by interaction with the Hsp70/Hdj1 system. In contrast, Hsp90 protects the DBD of p53 wild-type and mutant proteins from unfolding. We propose that the Hsp70 and Hsp90 chaperone systems assume complementary functions to optimally balance conformational plasticity with conformational stability. |
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| DOI: | doi:10.1016/j.molcel.2019.03.032 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext: https://doi.org/10.1016/j.molcel.2019.03.032 |
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| | Volltext: http://www.sciencedirect.com/science/article/pii/S1097276519302369 |
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| | DOI: https://doi.org/10.1016/j.molcel.2019.03.032 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | cancer |
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| | DNAJB1/Hdj1 |
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| | HSP90AB1/Hsp90β |
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| | HSPA1A/Hsp70 |
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| | p53 allostery |
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| | p53 cancer mutants |
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| | p53 DNA binding |
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| | p53 inactivation |
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| | protein dynamics |
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| | protein folding |
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| K10plus-PPN: | 1668011026 |
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| Verknüpfungen: | → Zeitschrift |
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Hsp70- and Hsp90-mediated regulation of the conformation of p53 DNA binding domain and p53 cancer variants / Boysen, Marta [VerfasserIn]; 23 April 2019 (Online-Ressource)
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