The interaction of versican with its binding partners.
Versican belongs to the family of the large aggregating chondroitin sulfate proteoglycans located primarily within the extracellular matrix (ECM). Versican, like other members of its family, has unique N- and C-terminal globular regions, each with multiple motifs. A large glycosaminoglycan-binding region lies between them. This review will begin by outlining these structures, in the context of ECM proteoglycans. The diverse binding partners afforded to versican by virtue of its modular design will then be examined. These include ECM components, such as hyaluronan, type I collagen, tenascin-R, fibulin-1, and -2, fibrillin-1, fibronectin, P- and L-selectins, and chemokines. Versican also binds to the cell surface proteins CD44, integrin beta 1, epidermal growth factor receptor, and P-selectin glycoprotein ligand-1. These multiple interactors play important roles in cell behaviour, and the roles of versican in modulating such processes are discussed.
Wu
Yao Jiong
YJ
Sunnybrook and Women's College Health Sciences Centre, 2075 Bayview Avenue, Toronto M4N 3M5 Canada.
La Pierre
David P
DP
Wu
Jin
J
Yee
Albert J
AJ
Yang
Burton B
BB
D000818:Animals; D011508:Chondroitin Sulfate Proteoglycans / Q000737:chemistry / Q000378:metabolism*; D005109:Extracellular Matrix / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D037181:Lectins, C-Type; D008565:Membrane Proteins / Q000378:metabolism; D011485:Protein Binding; D053675:Versicans
D011508:Chondroitin Sulfate Proteoglycans; D037181:Lectins, C-Type; D008565:Membrane Proteins; C508322:VCAN protein, human; D053675:Versicans