Syndecan-1 binds integrin alphaVbeta5

Stable Identifier
Reaction [binding]
Homo sapiens
SVG |   | PPTX  | SBGN
Syndecan-1 binds integrin alphaVbeta5

Syndecans have attached heparan sulfate (HS) and to a lesser extent chondroitin sulfate (CS) chains. These allow interactions with a large number of proteins. Various enzymes involved in post-translational HS chain modifications produce unique binding motifs that selectively recognize different proteins (Tkachenko et al. 2005). It is thought that syndecans often act in concert with other receptors, e.g. integrins alphavbeta3 and alphavbeta5 cooperate with syndecan-1 during adhesion to vitronectin (Beauvais et al. 2004, McQuade et al. 2006). The relationship between syndecans and co-receptors is not well understood (Alexopoulou et al. 2007). Syndecan-null mice have subtle phenotypes when compared with mice deficient in HS chain synthesis or modification (Echtermeyer et al. 2001, Ishiquro et al. 2001, Götte et al. 2002). GPI-anchored glypicans and matrix HSPGs such as perlecan may compensate for the absence of syndecans.

Literature References
PubMed ID Title Journal Year
16720645 Syndecan-1 regulates alphavbeta5 integrin activity in B82L fibroblasts

McQuade, KJ, Beauvais, DM, Burbach, BJ, Rapraeger, AC

J. Cell. Sci. 2006
Orthologous Events
Cross References
Target Pathogen
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