Discoidin Domain Receptors Promote α1β1- and α2β1-Integrin Mediated Cell Adhesion to Collagen by Enhancing Integrin Activation

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Huifang Xu; Dominique Bihan; Francis Chang; Paul H Huang; Richard W Farndale; Birgit Leitinger;
(2012)
  • Publisher: Public Library of Science
  • Journal: PLoS ONE, volume 7, issue 12 (issn: 1932-6203, eissn: 1932-6203)
  • Publisher copyright policies & self-archiving
  • Identifiers: doi: 10.1371/journal.pone.0052209, pmc: PMC3527415
  • Subject: Transmembrane Proteins | Signaling in Cellular Processes | Research Article | Biology | Molecular Cell Biology | Extracellular Matrix Proteins | Signal Transduction | Medicine | Extracellular Matrix Adhesions | Membrane Receptor Signaling | Q | R | Integrins | Proteins | Cell Adhesion | Science | Biochemistry | Transmembrane Signaling | Extracellular Matrix | Extracellular Matrix Signaling

The discoidin domain receptors, DDR1 and DDR2, are receptor tyrosine kinases that bind to and are activated by collagens. Similar to collagen-binding β1 integrins, the DDRs bind to specific motifs within the collagen triple helix. However, these two types of collagen re... View more