| First Author | Li R | Year | 2013 |
| Journal | J Thromb Haemost | Volume | 11 |
| Issue | 4 | Pages | 605-14 |
| PubMed ID | 23336709 | Mgi Jnum | J:320061 |
| Mgi Id | MGI:6867293 | Doi | 10.1111/jth.12144 |
| Citation | Li R, et al. (2013) The organizing principle of the platelet glycoprotein Ib-IX-V complex. J Thromb Haemost 11(4):605-14 |
| abstractText | The glycoprotein (GP)Ib-IX-V complex is the platelet receptor for von Willebrand factor and many other molecules that are critically involved in hemostasis and thrombosis. The lack of functional GPIb-IX-V complexes on the platelet surface is the cause of Bernard-Soulier syndrome, a rare hereditary bleeding disorder that is also associated with macrothrombocytopenia. GPIb-IX-V contains GPIbalpha, GPIbbeta, GPIX and GPV subunits, all of which are type I transmembrane proteins containing leucine-rich repeat domains. Although all of the subunits were identified decades ago, not until recently did the mechanism of complex assembly begin to emerge from a systematic characterization of inter-subunit interactions. This review summarizes the forces driving the assembly of GPIb-IX-V, discusses their implications for the pathogenesis of Bernard-Soulier syndrome, and identifies questions that remain about the structure and organization of GPIb-IX-V. |
