Structure of a collagen VI α3 chain VWA domain array: adaptability and functional implications of myopathy causing mutations.

VWA domain collagen collagen VI crystallography electron microscopy (EM) extracellular matrix extracellular matrix protein muscular dystrophy myopathy single-particle EM single-particle analysis small-angle X-ray scattering (SAXS)

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
04 09 2020
Historique:
received: 22 06 2020
revised: 16 07 2020
pubmed: 29 7 2020
medline: 28 1 2021
entrez: 29 7 2020
Statut: ppublish

Résumé

Collagen VI is a ubiquitous heterotrimeric protein of the extracellular matrix (ECM) that plays an essential role in the proper maintenance of skeletal muscle. Mutations in collagen VI lead to a spectrum of congenital myopathies, from the mild Bethlem myopathy to the severe Ullrich congenital muscular dystrophy. Collagen VI contains only a short triple helix and consists primarily of von Willebrand factor type A (VWA) domains, protein-protein interaction modules found in a range of ECM proteins. Disease-causing mutations occur commonly in the VWA domains, and the second VWA domain of the α3 chain, the N2 domain, harbors several such mutations. Here, we investigate structure-function relationships of the N2 mutations to shed light on their possible myopathy mechanisms. We determined the X-ray crystal structure of N2, combined with monitoring secretion efficiency in cell culture of selected N2 single-domain mutants, finding that mutations located within the central core of the domain severely affect secretion efficiency. In longer α3 chain constructs, spanning N6-N3, small-angle X-ray scattering demonstrates that the tandem VWA array has a modular architecture and samples multiple conformations in solution. Single-particle EM confirmed the presence of multiple conformations. Structural adaptability appears intrinsic to the VWA domain region of collagen VI α3 and has implications for binding interactions and modulating stiffness within the ECM.

Identifiants

pubmed: 32719005
pii: S0021-9258(17)49989-3
doi: 10.1074/jbc.RA120.014865
pmc: PMC7476709
doi:

Substances chimiques

COL6A3 protein, human 0
Collagen Type VI 0

Banques de données

PDB
['4IGI', '4CN8', '6SNK']

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

12755-12771

Subventions

Organisme : Medical Research Council
ID : MR/K018779/1
Pays : United Kingdom

Informations de copyright

© 2020 Solomon-Degefa et al.

Déclaration de conflit d'intérêts

Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article.

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Auteurs

Herimela Solomon-Degefa (H)

Center for Biochemistry, Medical Faculty, University of Cologne, Cologne, Germany.

Jan M Gebauer (JM)

Institute of Biochemistry, University of Cologne, Cologne, Germany.

Cy M Jeffries (CM)

European Molecular Biology Laboratory, Hamburg Unit, Hamburg, Germany.

Carolin D Freiburg (CD)

Center for Biochemistry, Medical Faculty, University of Cologne, Cologne, Germany.

Patrick Meckelburg (P)

Institute of Biochemistry, University of Cologne, Cologne, Germany.

Louise E Bird (LE)

The Research Complex at Harwell, Rutherford Appleton Laboratory Harwell, Oxford, United Kingdom.
Structural Biology Division, Wellcome Human Genetics Centre, University of Oxford, Oxford, United Kingdom.

Ulrich Baumann (U)

Institute of Biochemistry, University of Cologne, Cologne, Germany.

Dmitri I Svergun (DI)

European Molecular Biology Laboratory, Hamburg Unit, Hamburg, Germany.

Raymond J Owens (RJ)

The Research Complex at Harwell, Rutherford Appleton Laboratory Harwell, Oxford, United Kingdom.
Structural Biology Division, Wellcome Human Genetics Centre, University of Oxford, Oxford, United Kingdom.

Jörn M Werner (JM)

School of Biological Sciences, University of Southampton, Southampton, United Kingdom.

Elmar Behrmann (E)

Institute of Biochemistry, University of Cologne, Cologne, Germany.
Max Planck Research Group Structural Dynamics of Proteins, Center of Advanced European Studies and Research (caesar), Bonn, Germany.

Mats Paulsson (M)

Center for Biochemistry, Medical Faculty, University of Cologne, Cologne, Germany.
Center for Molecular Medicine (CMMC), Cologne, Germany.
Cologne Center for Musculoskeletal Biomechanics (CCMB), Cologne, Germany.

Raimund Wagener (R)

Center for Biochemistry, Medical Faculty, University of Cologne, Cologne, Germany raimund.wagener@uni-koeln.de.
Center for Molecular Medicine (CMMC), Cologne, Germany.
Cologne Center for Musculoskeletal Biomechanics (CCMB), Cologne, Germany.

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Classifications MeSH