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Article

Platelet glycoprotein Ib beta/IX mediates glycoprotein Ib alpha localization to membrane lipid domain critical for von Willebrand factor interaction at high shear.

The Journal of biological chemistry - 17 Jun 2011

Geng Hongquan, Xu Guofeng, Ran Yali, López José A, Peng Yuandong

Abstract excerpt

The localization of the platelet glycoprotein GP Ib-IX complex (GP Ibα, GP Ibβ, and GP IX) to membrane lipid domain, also known as glycosphingolipid-enriched membranes (GEMs or raft) lipid domain, is essential for the GP Ib-IX complex mediated platelet adhesion to von Willebrand factor (vWf) and subsequent platelet activation. To date, the mechanism for the complex association with the GEMs remains unclear....

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Source

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Identifiers

PMID: 21507943
DOI: 10.1074/jbc.M110.202549
PMCID: PMC3122191

Genes

GEM

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Platelet glycoprotein Ib beta/IX mediates glycoprotein Ib alpha localization to membrane lipid domain critical for von Willebrand factor interaction at high shear.PMID 21507943Read ↗

The Transmembrane Domains of β and IX Subunits Mediate the Localization of the Platelet Glycoprotein Ib-IX Complex to the Glycosphingolipid-enriched Membrane Domain.Semantic proximity Read ↗

Identification of three tyrosine residues of glycoprotein Ib alpha with distinct roles in von Willebrand factor and alpha-thrombin binding.Semantic proximity Read ↗

Role of the transmembrane domain of glycoprotein IX in assembly of the glycoprotein Ib-IX complex.Semantic proximity Read ↗

Identification of a novel 14-3-3zeta binding site within the cytoplasmic domain of platelet glycoprotein Ibalpha that plays a key role in regulating the von Willebrand factor binding function of glycoprotein Ib-IX.Semantic proximity Read ↗

The organizing principle of the platelet glycoprotein Ib-IX-V complex.Semantic proximity Read ↗

Surface expression of glycoprotein ib alpha is dependent on glycoprotein ib beta: evidence from a novel mutation causing Bernard-Soulier syndrome.Semantic proximity Read ↗

Juxtamembrane basic residues in glycoprotein Ibbeta cytoplasmic domain are required for assembly and surface expression of glycoprotein Ib-IX complex.Semantic proximity Read ↗

O-linked glycosylation of von Willebrand factor modulates the interaction with platelet receptor glycoprotein Ib under static and shear stress conditions.Semantic proximity Read ↗

Prediction of binding characteristics between von Willebrand factor and platelet glycoprotein Ibα with various mutations by molecular dynamic simulation.Semantic proximity Read ↗

Platelets with a W127X mutation in GPIX express sufficient residual amounts of GPIbα to support adhesion to von Willebrand factor and collagen.Semantic proximity Read ↗

Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain.Semantic proximity Read ↗

Interaction between GPIbalpha and FcgammaIIA receptor in human platelets.Semantic proximity Read ↗

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