FN1 dimer Integrin alphaVbeta1 Integrin alphaVbeta1:FN1 dimer Interaction of integrin alphaVbeta1 with Fibronectin Authored: Geiger, B, Horwitz, R, 2008-05-07 08:30:32 Edited: Garapati, P V, 2008-03-11 10:20:45 Pubmed10801899 Pubmed11997396 Pubmed1677003 Pubmed19285555 Pubmed20690820 Pubmed2380248 Reactome Database ID Release 43216314 Reactome, http://www.reactome.org ReactomeREACT_13423 Reviewed: Yamada, K, Humphries, MJ, Hynes, R, 2008-05-07 08:53:37 The alphaV integrin subfamily has five members, all recognize components of the ECM. AlphaVbeta1 integrin binds fibronectin (FN1). In solution FN1 occurs as a dimer. Binding to alpha5beta1 integrin stimulates FN1 self-association; blocking the RGD-cell binding domain of FN1 blocks fibril formation (Fogerty et al. 1990). FN1 binding is believed to induce integrin clustering, which promotes FN1-FN1 interactions. Integrin clustering is mediated by association between integrins and intracellular actin stress fibers (Calderwood et al. 2000). Binding of integrins to each of the monomers in the FN1 dimer pair is thought to trigger a conformational change in FN1 that exposes 'cryptic' FN1 binding sites that allow additional fibronectin dimers to bind without the requirement for preassociation with integrins (Singh et al. 2010). This non-covalent interaction may involve interactions with fibrillin (Ohashi & Erickson 2009). I1-5 functions as a unit that is the primary FN matrix assembly domain (Sottile et al. 1991) but other units are likely to be involved (Singh et al. 2010), the process is not fully understood. has a Stoichiometric coefficient of 2