دورية أكاديمية

Adapting Secretory Proteostasis and Function Through the Unfolded Protein Response.

التفاصيل البيبلوغرافية
العنوان: Adapting Secretory Proteostasis and Function Through the Unfolded Protein Response.
المؤلفون: Wong MY; Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Ave, Cambridge, MA, 02139-4307, USA., DiChiara AS; Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Ave, Cambridge, MA, 02139-4307, USA., Suen PH; Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Ave, Cambridge, MA, 02139-4307, USA., Chen K; Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Ave, Cambridge, MA, 02139-4307, USA., Doan ND; Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Ave, Cambridge, MA, 02139-4307, USA., Shoulders MD; Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Ave, Cambridge, MA, 02139-4307, USA. mshoulde@mit.edu.
المصدر: Current topics in microbiology and immunology [Curr Top Microbiol Immunol] 2018; Vol. 414, pp. 1-25.
نوع المنشور: Journal Article; Review
اللغة: English
بيانات الدورية: Publisher: Springer Verlag Country of Publication: Germany NLM ID: 0110513 Publication Model: Print Cited Medium: Print ISSN: 0070-217X (Print) Linking ISSN: 0070217X NLM ISO Abbreviation: Curr Top Microbiol Immunol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Heidelberg : Springer Verlag
مواضيع طبية MeSH: Proteostasis/*physiology , Unfolded Protein Response/*physiology, Animals ; Endoplasmic Reticulum/metabolism ; Humans ; Protein Folding
مستخلص: Cells address challenges to protein folding in the secretory pathway by engaging endoplasmic reticulum (ER)-localized protective mechanisms that are collectively termed the unfolded protein response (UPR). By the action of the transmembrane signal transducers IRE1, PERK, and ATF6, the UPR induces networks of genes whose products alleviate the burden of protein misfolding. The UPR also plays instructive roles in cell differentiation and development, aids in the response to pathogens, and coordinates the output of professional secretory cells. These functions add to and move beyond the UPR's classical role in addressing proteotoxic stress. Thus, the UPR is not just a reaction to protein misfolding, but also a fundamental driving force in physiology and pathology. Recent efforts have yielded a suite of chemical genetic methods and small molecule modulators that now provide researchers with both stress-dependent and -independent control of UPR activity. Such tools provide new opportunities to perturb the UPR and thereby study mechanisms for maintaining proteostasis in the secretory pathway. Numerous observations now hint at the therapeutic potential of UPR modulation for diseases related to the misfolding and aggregation of ER client proteins. Growing evidence also indicates the promise of targeting ER proteostasis nodes downstream of the UPR. Here, we review selected advances in these areas, providing a resource to inform ongoing studies of secretory proteostasis and function as they relate to the UPR.
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معلومات مُعتمدة: R01 AR071443 United States AR NIAMS NIH HHS
تواريخ الأحداث: Date Created: 20170921 Date Completed: 20180920 Latest Revision: 20191008
رمز التحديث: 20240829
مُعرف محوري في PubMed: PMC5860992
DOI: 10.1007/82_2017_56
PMID: 28929194
قاعدة البيانات: MEDLINE
الوصف
تدمد:0070-217X
DOI:10.1007/82_2017_56