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Interaction of discoidin domain receptor 1 with collagen type 1

Gunjan Agarwal1, Cosmin Mihai, Daniel F Iscru

  • 1Davis Heart and Lung Research Institute, Ohio State University, Columbus, OH 43210, USA. agarwal.60@osu.edu

Journal of Molecular Biology
|February 6, 2007
PubMed

Insights

Discoidin domain receptor 1 (DDR1) oligomers bind collagen type 1, altering fibril formation. This interaction, mediated by the DDR1 extracellular domain (ECD), impacts collagen structure and function.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Discoidin domain receptor 1 (DDR1) is a tyrosine kinase receptor that interacts with collagens.
  • The precise binding mechanism and functional consequences of DDR1-collagen interactions remain largely uncharacterized.

Purpose of the Study:

  • To investigate the binding pattern of the DDR1 extracellular domain (ECD) to collagen type 1.
  • To determine the impact of DDR1-collagen interaction on collagen fibrillogenesis.

Main Methods:

  • Utilized DDR1-Fc fusion proteins containing the DDR1 ECD for in vitro assays.
  • Employed surface plasmon resonance (SPR) to assess binding affinity.
  • Applied atomic force microscopy (AFM) for single-molecule imaging of DDR1-collagen interactions.
  • Conducted cell-based assays to evaluate effects on collagen fibrillogenesis.

Main Results:

  • DDR1 oligomerization significantly enhanced binding to collagen type 1.
  • DDR1 oligomers preferentially bound to overlapping or adjacent collagen molecules, not isolated ones.
  • DDR1 interaction modulated collagen fibrillogenesis, resulting in larger diameter, more cross-linked fibers lacking native banding.
  • DDR1 ECD induced a "locked" state in collagen molecules, hindering complete fibril formation.

Conclusions:

  • The DDR1 ECD plays a crucial role in modulating collagen fibrillogenesis.
  • This interaction represents a novel mechanism for DDR1-mediated collagen regulation.
  • Findings are relevant to kinase-dead DDR1 isoforms and soluble shed DDR1 ECD.

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