Structural basis of homo- and heterotrimerization of collagen I

Urvashi Sharma, Loïc Carrique, Sandrine Vadon-Le Goff, Natacha Mariano, Rainier-Numa Georges, Frederic Delolme, Peppi Koivunen, Johanna Myllyharju, Catherine Moali, Nushin Aghajari () and David J. S. Hulmes ()
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Urvashi Sharma: Molecular Microbiology and Structural Biochemistry Unit, UMR 5086 CNRS - University of Lyon 1
Loïc Carrique: Molecular Microbiology and Structural Biochemistry Unit, UMR 5086 CNRS - University of Lyon 1
Sandrine Vadon-Le Goff: Tissue Biology and Therapeutic Engineering Unit, UMR 5305 CNRS - University of Lyon 1
Natacha Mariano: Tissue Biology and Therapeutic Engineering Unit, UMR 5305 CNRS - University of Lyon 1
Rainier-Numa Georges: Tissue Biology and Therapeutic Engineering Unit, UMR 5305 CNRS - University of Lyon 1
Frederic Delolme: Tissue Biology and Therapeutic Engineering Unit, UMR 5305 CNRS - University of Lyon 1
Peppi Koivunen: Oulu Center for Cell-Matrix Research, Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu
Johanna Myllyharju: Oulu Center for Cell-Matrix Research, Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu
Catherine Moali: Tissue Biology and Therapeutic Engineering Unit, UMR 5305 CNRS - University of Lyon 1
Nushin Aghajari: Molecular Microbiology and Structural Biochemistry Unit, UMR 5086 CNRS - University of Lyon 1
David J. S. Hulmes: Tissue Biology and Therapeutic Engineering Unit, UMR 5305 CNRS - University of Lyon 1

Nature Communications, 2017, vol. 8, issue 1, 1-10

Abstract: Abstract Fibrillar collagen molecules are synthesized as precursors, procollagens, with large propeptide extensions. While a homotrimeric form (three α1 chains) has been reported in embryonic tissues as well as in diseases (cancer, fibrosis, genetic disorders), collagen type I usually occurs as a heterotrimer (two α1 chains and one α2 chain). Inside the cell, the role of the C-terminal propeptides is to gather together the correct combination of three α chains during molecular assembly, but how this occurs for different forms of the same collagen type is so far unknown. Here, by structural and mutagenic analysis, we identify key amino acid residues in the α1 and α2 C-propeptides that determine homo- and heterotrimerization. A naturally occurring mutation in one of these alters the homo/heterotrimer balance. These results show how the C-propeptide of the α2 chain has specifically evolved to permit the appearance of heterotrimeric collagen I, the major extracellular building block among the metazoa.

Date: 2017
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DOI: 10.1038/ncomms14671

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