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Integrin recognition motifs in the human collagens
Samir Hamaia1, Richard W Farndale
1Department of Biochemistry, Cambridge University, Downing Site, Cambridge, CB2 1QW, UK.
Advances in Experimental Medicine and Biology
|July 16, 2014
Summary
Cellular adhesion relies on specific collagen sequences recognized by integrins. Variations in these Gxx
Area of Science:
- Biochemistry
- Cell Biology
- Structural Biology
Background:
- Fibrillar collagens mediate cellular adhesion via specific collagen-binding integrins.
- Key integrins include α1β1, α2β1, α10β1, and α11β1, recognizing distinct collagen sequences.
Purpose of the Study:
- To review sequence variations supporting integrin reactivity across human collagens.
- To analyze the distribution of these motifs within the 28 human collagen types.
Main Methods:
- Analysis of triple-helical, homotrimeric collagen peptides.
- Review of existing literature on integrin-collagen interactions.
Main Results:
- Identified Gxx'GEx'' motifs (x=hydrophobic, x'=hydroxyproline, x''=arginine/lysine) as critical for integrin binding.
- Fibrillar collagens I, II, and III are rich in GxOGER motifs.
- GxOGEK motifs are more widely distributed but less common in fibrillar collagens I, II, and III.
Conclusions:
- Sequence variations within collagen motifs dictate integrin binding specificity.
- Both homotrimeric and heterotrimeric collagens can support integrin-mediated adhesion.
- Understanding these motifs is crucial for comprehending cell-matrix interactions.
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