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Giantin is required for intracellular N-terminal processing of type I procollagen

View ORCID ProfileNicola L. Stevenson, View ORCID ProfileJ. M. Bergen Dylan, View ORCID ProfileChrissy L. Hammond, View ORCID ProfileDavid J. Stephens
doi: https://doi.org/10.1101/2020.05.25.115279
Nicola L. Stevenson
1Cell Biology Laboratories, School of Biochemistry, Faculty of Life Sciences, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK
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J. M. Bergen Dylan
2School of Physiology, Pharmacology and Neuroscience, Faculty of Life Sciences, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK
3Musculoskeletal Research Unit, Translational Health Sciences, Bristol Medical School, Faculty of Health Sciences, University of Bristol, Southmead Hospital, Bristol, BS10 5NB, UK
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Chrissy L. Hammond
2School of Physiology, Pharmacology and Neuroscience, Faculty of Life Sciences, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK
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David J. Stephens
1Cell Biology Laboratories, School of Biochemistry, Faculty of Life Sciences, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK
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  • For correspondence: david.stephens@bristol.ac.uk
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Abstract

Knockout of the golgin giantin leads to skeletal and craniofacial defects driven by poorly studied changes in glycosylation and extracellular matrix deposition. Here, we sought to determine how giantin impacts the production of healthy bone tissue by focussing on the main protein component of the osteoid, type I collagen. Giantin mutant zebrafish accumulate multiple spontaneous fractures in their caudal fin, suggesting their bones may be more brittle. Inducing new experimental fractures revealed defects in the mineralisation of newly deposited collagen as well as diminished procollagen reporter expression in mutant fish. Analysis of giantin knockout cells expressing a GFP-tagged procollagen showed that procollagen trafficking is independent of giantin. However, our data show that intracellular N-propeptide processing of pro-α1(I) is defective in the absence of giantin. These data demonstrate a conserved role for giantin in collagen biosynthesis and extracellular matrix assembly. Our work also provides evidence of a giantin-dependent pathway for intracellular procollagen processing.

Competing Interest Statement

The authors have declared no competing interest.

Footnotes

  • Reference list and online title corrected.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted May 26, 2020.
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Giantin is required for intracellular N-terminal processing of type I procollagen
Nicola L. Stevenson, J. M. Bergen Dylan, Chrissy L. Hammond, David J. Stephens
bioRxiv 2020.05.25.115279; doi: https://doi.org/10.1101/2020.05.25.115279
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Giantin is required for intracellular N-terminal processing of type I procollagen
Nicola L. Stevenson, J. M. Bergen Dylan, Chrissy L. Hammond, David J. Stephens
bioRxiv 2020.05.25.115279; doi: https://doi.org/10.1101/2020.05.25.115279

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