دورية أكاديمية
The Essential Functions of Molecular Chaperones and Folding Enzymes in Maintaining Endoplasmic Reticulum Homeostasis.
| العنوان: | The Essential Functions of Molecular Chaperones and Folding Enzymes in Maintaining Endoplasmic Reticulum Homeostasis. |
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| المؤلفون: | Hendershot LM; Department of Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, United States. Electronic address: linda.hendershot@stjude.org., Buck TM; Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States., Brodsky JL; Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States. |
| المصدر: | Journal of molecular biology [J Mol Biol] 2024 Jul 15; Vol. 436 (14), pp. 168418. Date of Electronic Publication: 2023 Dec 22. |
| نوع المنشور: | Journal Article; Review |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: Netherlands NLM ID: 2985088R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1089-8638 (Electronic) Linking ISSN: 00222836 NLM ISO Abbreviation: J Mol Biol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Amsterdam : Elsevier Original Publication: 1959- : London : Academic Press |
| مواضيع طبية MeSH: | Endoplasmic Reticulum*/metabolism , Molecular Chaperones*/metabolism , Molecular Chaperones*/chemistry , Molecular Chaperones*/genetics , Protein Folding* , Homeostasis*, Humans ; Animals |
| مستخلص: | It has been estimated that up to one-third of the proteins encoded by the human genome enter the endoplasmic reticulum (ER) as extended polypeptide chains where they undergo covalent modifications, fold into their native structures, and assemble into oligomeric protein complexes. The fidelity of these processes is critical to support organellar, cellular, and organismal health, and is perhaps best underscored by the growing number of disease-causing mutations that reduce the fidelity of protein biogenesis in the ER. To meet demands encountered by the diverse protein clientele that mature in the ER, this organelle is populated with a cadre of molecular chaperones that prevent protein aggregation, facilitate protein disulfide isomerization, and lower the activation energy barrier of cis-trans prolyl isomerization. Components of the lectin (glycan-binding) chaperone system also reside within the ER and play numerous roles during protein biogenesis. In addition, the ER houses multiple homologs of select chaperones that can recognize and act upon diverse peptide signatures. Moreover, redundancy helps ensure that folding-compromised substrates are unable to overwhelm essential ER-resident chaperones and enzymes. In contrast, the ER in higher eukaryotic cells possesses a single member of the Hsp70, Hsp90, and Hsp110 chaperone families, even though several homologs of these molecules reside in the cytoplasm. In this review, we discuss specific functions of the many factors that maintain ER quality control, highlight some of their interactions, and describe the vulnerabilities that arise from the absence of multiple members of some chaperone families. Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. (Copyright © 2023 Elsevier Ltd. All rights reserved.) |
| معلومات مُعتمدة: | R01 DK117126 United States DK NIDDK NIH HHS |
| فهرسة مساهمة: | Keywords: chaperones; co-chaperones; protein folding; proteostasis; unfolded protein response (UPR) |
| المشرفين على المادة: | 0 (Molecular Chaperones) |
| تواريخ الأحداث: | Date Created: 20231224 Date Completed: 20240627 Latest Revision: 20240701 |
| رمز التحديث: | 20240701 |
| DOI: | 10.1016/j.jmb.2023.168418 |
| PMID: | 38143019 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1089-8638 |
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| DOI: | 10.1016/j.jmb.2023.168418 |