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Structural basis of substrate recognition and allosteric activation of the proapoptotic mitochondrial HtrA2 protease.

التفاصيل البيبلوغرافية
العنوان: Structural basis of substrate recognition and allosteric activation of the proapoptotic mitochondrial HtrA2 protease.
المؤلفون: Aspholm EE; Department of Chemistry and Molecular Biology, University of Gothenburg, Göteborg, Sweden.; Wallenberg Centre for Molecular and Translational Medicine, University of Gothenburg, Göteborg, Sweden., Lidman J; Department of Chemistry and Molecular Biology, University of Gothenburg, Göteborg, Sweden.; Wallenberg Centre for Molecular and Translational Medicine, University of Gothenburg, Göteborg, Sweden., Burmann BM; Department of Chemistry and Molecular Biology, University of Gothenburg, Göteborg, Sweden. bjorn.marcus.burmann@gu.se.; Wallenberg Centre for Molecular and Translational Medicine, University of Gothenburg, Göteborg, Sweden. bjorn.marcus.burmann@gu.se.
المصدر: Nature communications [Nat Commun] 2024 May 30; Vol. 15 (1), pp. 4592. Date of Electronic Publication: 2024 May 30.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE
أسماء مطبوعة: Original Publication: [London] : Nature Pub. Group
مواضيع طبية MeSH: High-Temperature Requirement A Serine Peptidase 2*/metabolism , High-Temperature Requirement A Serine Peptidase 2*/genetics , Apoptosis* , PDZ Domains*, Humans ; Allosteric Regulation ; Substrate Specificity ; Mitochondria/metabolism ; Models, Molecular ; Magnetic Resonance Spectroscopy
مستخلص: The mitochondrial serine protease HtrA2 is a human homolog of the Escherichia coli Deg-proteins exhibiting chaperone and proteolytic roles. HtrA2 is involved in both apoptotic regulation via its ability to degrade inhibitor-of-apoptosis proteins (IAPs), as well as in cellular maintenance as part of the cellular protein quality control machinery, by preventing the possible toxic accumulation of aggregated proteins. In this study, we use advanced solution NMR spectroscopy methods combined with biophysical characterization and biochemical assays to elucidate the crucial role of the substrate recognizing PDZ domain. This domain regulates the protease activity of HtrA2 by triggering an intricate allosteric network involving the regulatory loops of the protease domain. We further show that divalent metal ions can both positively and negatively modulate the activity of HtrA2, leading to a refined model of HtrA2 regulation within the apoptotic pathway.
(© 2024. The Author(s).)
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معلومات مُعتمدة: 2019-0415 Cancerfonden (Swedish Cancer Society); 2022-2490 Cancerfonden (Swedish Cancer Society); 2016.0163 Knut och Alice Wallenbergs Stiftelse (Knut and Alice Wallenberg Foundation); 2020.0300 Knut och Alice Wallenbergs Stiftelse (Knut and Alice Wallenberg Foundation); 2020-00466 Vetenskapsrådet (Swedish Research Council)
المشرفين على المادة: EC 3.4.21.108 (High-Temperature Requirement A Serine Peptidase 2)
EC 3.4.21.108 (HTRA2 protein, human)
تواريخ الأحداث: Date Created: 20240530 Date Completed: 20240530 Latest Revision: 20240530
رمز التحديث: 20240531
DOI: 10.1038/s41467-024-48997-5
PMID: 38816423
قاعدة البيانات: MEDLINE
الوصف
تدمد:2041-1723
DOI:10.1038/s41467-024-48997-5