Skelemin association with αIIbβ3 integrin: a structural model

Biochemistry. 2014 Nov 4;53(43):6766-75. doi: 10.1021/bi500680s. Epub 2014 Oct 22.

Abstract

Over the last two decades, our knowledge concerning intracellular events that regulate integrin's affinity to their soluble ligands has significantly improved. However, the mechanism of adhesion-induced integrin clustering and development of focal complexes, which could further mature to form focal adhesions, still remains under-investigated. Here we present a structural model of tandem IgC2 domains of skelemin in complex with the cytoplasmic tails of integrin αIIbβ3. The model of tertiary assembly is generated based upon NMR data and illuminates a potential link between the essential cell adhesion receptors and myosin filaments. This connection may serve as a basis for generating the mechanical forces necessary for cell migration and remodeling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Connectin / chemistry*
  • Humans
  • Mice
  • Models, Molecular*
  • Platelet Glycoprotein GPIIb-IIIa Complex / chemistry*
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary

Substances

  • Connectin
  • Myom1 protein, mouse
  • Platelet Glycoprotein GPIIb-IIIa Complex

Grants and funding

National Institutes of Health, United States