دورية أكاديمية
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Chaperone BiP controls ER stress sensor Ire1 through interactions with its oligomers.

التفاصيل البيبلوغرافية
العنوان: Chaperone BiP controls ER stress sensor Ire1 through interactions with its oligomers.
المؤلفون: Dawes S; https://ror.org/024mrxd33 School of Molecular and Cellular Biology, Faculty of Biological Sciences & Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK.; Chemistry Department, University of Sheffield, Sheffield, UK., Hurst N; https://ror.org/024mrxd33 School of Molecular and Cellular Biology, Faculty of Biological Sciences & Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK., Grey G; https://ror.org/024mrxd33 School of Molecular and Cellular Biology, Faculty of Biological Sciences & Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK., Wieteska L; https://ror.org/024mrxd33 School of Molecular and Cellular Biology, Faculty of Biological Sciences & Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK., Wright NV; https://ror.org/024mrxd33 School of Molecular and Cellular Biology, Faculty of Biological Sciences & Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK., Manfield IW; https://ror.org/024mrxd33 School of Molecular and Cellular Biology, Faculty of Biological Sciences & Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK., Hussain MH; https://ror.org/024mrxd33 School of Molecular and Cellular Biology, Faculty of Biological Sciences & Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK., Kalverda AP; https://ror.org/024mrxd33 School of Molecular and Cellular Biology, Faculty of Biological Sciences & Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK., Lewandowski JR; Department of Chemistry, University of Warwick, Coventry, UK., Chen B; Chemistry Department, University of Sheffield, Sheffield, UK., Zhuravleva A; https://ror.org/024mrxd33 School of Molecular and Cellular Biology, Faculty of Biological Sciences & Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK a.zhuravleva@leeds.ac.uk.
المصدر: Life science alliance [Life Sci Alliance] 2024 Aug 05; Vol. 7 (10). Date of Electronic Publication: 2024 Aug 05 (Print Publication: 2024).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Life Science Alliance, LLC Country of Publication: United States NLM ID: 101728869 Publication Model: Electronic-Print Cited Medium: Internet ISSN: 2575-1077 (Electronic) Linking ISSN: 25751077 NLM ISO Abbreviation: Life Sci Alliance Subsets: MEDLINE
أسماء مطبوعة: Original Publication: [Woodbury, NY] : Life Science Alliance, LLC, [2018]-
مواضيع طبية MeSH: Protein Serine-Threonine Kinases*/metabolism , Endoplasmic Reticulum Stress* , Endoplasmic Reticulum Chaperone BiP*/metabolism , Protein Binding* , Heat-Shock Proteins*/metabolism , Heat-Shock Proteins*/chemistry , Endoribonucleases*/metabolism , Endoribonucleases*/chemistry, Humans ; Endoplasmic Reticulum/metabolism ; Unfolded Protein Response ; Protein Multimerization ; HSP70 Heat-Shock Proteins/metabolism ; HSP70 Heat-Shock Proteins/chemistry ; Protein Folding ; Molecular Chaperones/metabolism ; Molecular Chaperones/chemistry ; Protein Domains
مستخلص: The complex multistep activation cascade of Ire1 involves changes in the Ire1 conformation and oligomeric state. Ire1 activation enhances ER folding capacity, in part by overexpressing the ER Hsp70 molecular chaperone BiP; in turn, BiP provides tight negative control of Ire1 activation. This study demonstrates that BiP regulates Ire1 activation through a direct interaction with Ire1 oligomers. Particularly, we demonstrated that the binding of Ire1 luminal domain (LD) to unfolded protein substrates not only trigger conformational changes in Ire1-LD that favour the formation of Ire1-LD oligomers but also exposes BiP binding motifs, enabling the molecular chaperone BiP to directly bind to Ire1-LD in an ATP-dependent manner. These transient interactions between BiP and two short motifs in the disordered region of Ire1-LD are reminiscent of interactions between clathrin and another Hsp70, cytoplasmic Hsc70. BiP binding to substrate-bound Ire1-LD oligomers enables unfolded protein substrates and BiP to synergistically and dynamically control Ire1-LD oligomerisation, helping to return Ire1 to its deactivated state when an ER stress response is no longer required.
(© 2024 Dawes et al.)
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معلومات مُعتمدة: United Kingdom WT_ Wellcome Trust; FC001029 United Kingdom ARC_ Arthritis Research UK
سلسلة جزيئية: PDB 2HZ6; 6SHC
المشرفين على المادة: EC 2.7.11.1 (Protein Serine-Threonine Kinases)
0 (Endoplasmic Reticulum Chaperone BiP)
0 (Heat-Shock Proteins)
EC 3.1.- (Endoribonucleases)
EC 2.7.11.1 (ERN1 protein, human)
0 (HSP70 Heat-Shock Proteins)
0 (Molecular Chaperones)
تواريخ الأحداث: Date Created: 20240805 Date Completed: 20240805 Latest Revision: 20240808
رمز التحديث: 20240808
مُعرف محوري في PubMed: PMC11300964
DOI: 10.26508/lsa.202402702
PMID: 39103227
قاعدة البيانات: MEDLINE
الوصف
تدمد:2575-1077
DOI:10.26508/lsa.202402702