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New specific HSP47 ...
New specific HSP47 functions in collagen subfamily chaperoning
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- Köhler, Anna (author)
- University of Cologne
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- Mörgelin, Matthias (author)
- Lund University,Lunds universitet,Infektionsmedicin,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Infection Medicine (BMC),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine,Colzyx AB
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- Gebauer, Jan M. (author)
- University of Cologne
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- Öcal, Sinan (author)
- University of Cologne
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- Imhof, Thomas (author)
- University of Cologne
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- Koch, Manuel (author)
- University of Cologne
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- Nagata, Kazuhiro (author)
- Kyoto Sangyo University
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- Paulsson, Mats (author)
- University of Cologne
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- Zaucke, Frank (author)
- University Hospital Frankfurt
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- Baumann, Ulrich (author)
- University of Cologne
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- Sengle, Gerhard (author)
- University of Cologne,University Hospital of Cologne
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(creator_code:org_t)
- 2020
- 2020
- English 13 s.
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In: FASEB Journal. - 0892-6638. ; 34:9, s. 12040-12052
- Related links:
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http://dx.doi.org/10...
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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Abstract
Subject headings
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- Although collagens are the most abundant proteins implicated in various disease pathways, essential mechanisms required for their proper folding and assembly are poorly understood. Heat-shock protein 47 (HSP47), an ER-resident chaperone, was mainly reported to fulfill key functions in folding and secretion of fibrillar collagens by stabilizing pro-collagen triple-helices. In this study, we demonstrate unique functions of HSP47 for different collagen subfamilies. Our results show that HSP47 binds to the N-terminal region of procollagen I and is essential for its secretion. However, HSP47 ablation does not majorly impact collagen VI secretion, but its lateral assembly. Moreover, specific ablation of Hsp47 in murine keratinocytes revealed a new role for the transmembrane collagen XVII triple-helix formation. Incompletely folded collagen XVII C-termini protruding from isolated HSP47 null keratinocyte membrane vesicles could be fully restored upon the application of recombinant HSP47. Thus, our study expands the current view regarding the client repertoire and function of HSP47, as well as emphasizes its importance for transmembrane collagen folding.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
Keyword
- collagen
- collagen XVII
- FACIT
- HSP47
- MACIT
Publication and Content Type
- art (subject category)
- ref (subject category)
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- By the author/editor
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Köhler, Anna
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Mörgelin, Matthi ...
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Gebauer, Jan M.
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Öcal, Sinan
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Imhof, Thomas
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Koch, Manuel
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show more...
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Nagata, Kazuhiro
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Paulsson, Mats
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Zaucke, Frank
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Baumann, Ulrich
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Sengle, Gerhard
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show less...
- About the subject
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- MEDICAL AND HEALTH SCIENCES
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MEDICAL AND HEAL ...
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and Basic Medicine
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and Cell and Molecul ...
- Articles in the publication
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FASEB Journal
- By the university
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Lund University