ArticleJournal of thrombosis and haemostasis : JTH2020
Unaccompanied mechanosensory domain mediates low expression of glycoprotein Ibα: implications for Bernard-Soulier syndrome.
Article in Journal of thrombosis and haemostasis : JTH, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The trial behind it
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Specific O-glycans in the mechanosensory domain of glycoprotein Ibα are important for its stability and function.Haematologica · 2023Article
- 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
- A Novel Mutation inInternational journal of molecular sciences · 2021Article
- Structure-function of platelet glycoprotein Ib-IX.Journal of thrombosis and haemostasis : JTH · 2020Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundDisruption of protein folding or inter-subunit interactions in the platelet glycoprotein (GP)Ib-IX complex leads to its abnormally low expression in the plasma membrane, the hallmark of Bernard-Soulier syndrome (BSS).
objectiveTo discover the molecular mechanism by which GPIbα in the absence of GPIbβ and GPIX subunits is targeted for rapid degradation.
methodThe expression of GPIbα mutants with deletion or replacement of various domains were measured in transiently transfected Chinese hamster ovary cells.
resultsWe report evidence to suggest that induction of the unfolded protein response by the unaccompanied mechanosensory domain (MSD) is a major factor for intracellular degradation and low expression of GPIbα. Removal of the MSD produced the first GPIbα variant that, even in the absence of GPIbβ and GPIX, expressed at a level comparable to that of wild-type GPIbα in the GPIb-IX complex, while retaining its native ligand-binding activity.
conclusionOur finding has important implications on the molecular pathogenesis of BSS and the function of the GPIb-IX complex.
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Registered trials
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