ArticleJournal of thrombosis and haemostasis : JTH2014
Analysis of inter-subunit contacts reveals the structural malleability of extracellular domains in platelet glycoprotein Ib-IX complex.
Article in Journal of thrombosis and haemostasis : JTH, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Direct Binding of Lyn to GPIbβ Transmits 2-Way GPIb-IX Signaling to Stimulate Platelet Activation and VWF Binding.Circulation research · 2025Article
- The GPIb-IX complex on platelets: insight into its novel physiological functions affecting immune surveillance, hepatic thrombopoietin generation, platelet clearance and its relevance for cancer development and metastasis.Experimental hematology & oncology · 2022Review
- Differential regulation of the platelet GPIb-IX complex by anti-GPIbβ antibodies.Journal of thrombosis and haemostasis : JTH · 2021Article
- Structure-function of platelet glycoprotein Ib-IX.Journal of thrombosis and haemostasis : JTH · 2020Review
- Unaccompanied mechanosensory domain mediates low expression of glycoprotein Ibα: implications for Bernard-Soulier syndrome.Journal of thrombosis and haemostasis : JTH · 2020Article
- Platelet clearance via shear-induced unfolding of a membrane mechanoreceptor.Nature communications · 2016Article
- The Transmembrane Domains of β and IX Subunits Mediate the Localization of the Platelet Glycoprotein Ib-IX Complex to the Glycosphingolipid-enriched Membrane Domain.The Journal of biological chemistry · 2015Article
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Authors and funding
3 authors.
Funding
Abstract
backgroundThe glycoprotein (GP)Ib-IX complex is critical to hemostasis and thrombosis. Its proper assembly is closely correlated with its surface expression level and requires cooperative interactions among extracellular and transmembrane domains of Ibα, Ibβ and IX subunits. Two interfaces have been previously identified between the extracellular domains of Ibβ and IX.
objectiveTo understand how extracellular domains interact in GPIb-IX.
methodsThe Ibβ extracellular domain (IbβE ) or the IX counterpart (IXE ) in GPIb-IX was replaced with a well-folded IbβE /IXE chimera called IbβEabc , and the effect of domain replacement on assembly and expression of the receptor complex in transiently transfected Chinese hamster ovary cells was analyzed.
resultsReplacing IXE with IbβEabc in GPIb-IX retained interface 1 but not interface 2 between the extracellular domains. While this domain replacement preserved complex integrity, the expression levels of Ibβ and Ibα were significantly reduced. Additional domain replacement with IbβEabc or IbβE in GPIb-IX produced the complex at disparate expression levels that cannot be simply explained by two separate interfaces. In particular, when IbβE in GPIb-IX was replaced by IbβEabc , Ibα and IX were expressed at approximately 70% of the wild-type level. Their levels were not reduced when IXE was changed further to IbβE .
conclusionsOur results demonstrate the importance of the association between Ibβ and IX extracellular domains for complex assembly and efficient expression, and provide evidence for the structural malleability of these domains that may accommodate and propagate conformational changes therein.
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