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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Delineation of the region in the glycoprotein VI tail required for association with the Fc receptor gamma-chain.

The glycoprotein VI (GPVI).Fc receptor gamma-chain (FcRgamma-chain) complex is the major activation receptor for collagen on platelets. GPVI cross- linking mediates activation through tyrosine phosphorylation of an ITAM (immunoreceptor tyrosine-based activation motif) in the FcR gamma-chain by Src family kinases. It has been previously shown that a transmembrane arginine and the cytoplasmic domain of GPVI are required for association with the FcR gamma-chain in immortalized cell lines. In this study, we have delineated the regions in the GPVI tail that promote binding to FcR gamma-chain and mediate functional responses to the snake venom convulxin by reconstitution of mutant forms of GPVI in RBL-2H3 cells. Sequential truncation of the cytoplasmic tail of GPVI revealed a major role for the basic region and a minor role for the juxtamembrane six amino acids in the association with FcR gamma-chain and functional responses to convulxin. Analysis of selective deletions in the GPVI tail supported this conclusion. In addition, we show that the proline-rich domain is required for optimal Ca2+ release, whereas it is dispensable for FcR gamma-chain association.[1]

References

  1. Delineation of the region in the glycoprotein VI tail required for association with the Fc receptor gamma-chain. Bori-Sanz, T., Inoue, K.S., Berndt, M.C., Watson, S.P., Tulasne, D. J. Biol. Chem. (2003) [Pubmed]
 
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