New specific HSP47 functions in collagen subfamily chaperoning

Research output: Contribution to journalArticle


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.


  • Anna Köhler
  • Matthias Mörgelin
  • Jan M. Gebauer
  • Sinan Öcal
  • Thomas Imhof
  • Manuel Koch
  • Kazuhiro Nagata
  • Mats Paulsson
  • Frank Zaucke
  • Ulrich Baumann
  • Gerhard Sengle
External organisations
  • University of Cologne
  • Colzyx AB
  • Kyoto Sangyo University
  • University Hospital Frankfurt
  • University Hospital of Cologne
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Cell and Molecular Biology


  • collagen, collagen XVII, FACIT, HSP47, MACIT
Original languageEnglish
Pages (from-to)12040-12052
Number of pages13
JournalFASEB Journal
Issue number9
Early online date2020 Jul 27
Publication statusPublished - 2020 Sep
Publication categoryResearch