ArticleThe Journal of biological chemistry2010
Transmembrane and trans-subunit regulation of ectodomain shedding of platelet glycoprotein Ibalpha.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Platelet CLEC-2 activation leads to GPIb⍺ shedding: Implications for doxorubicin chemotherapy and thrombosis.The Journal of biological chemistry · 2026Article
- Unaccompanied mechanosensory domain mediates low expression of glycoprotein Ibα: implications for Bernard-Soulier syndrome.Journal of thrombosis and haemostasis : JTH · 2020Article
- Signaling Pathways of Receptors Involved in Platelet Activation and Shedding of These Receptors in Stored Platelets.Advanced pharmaceutical bulletin · 2019Review
- Proteolytic processing of platelet receptors.Research and practice in thrombosis and haemostasis · 2018Article
- 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
- Specific inhibition of ectodomain shedding of glycoprotein Ibα by targeting its juxtamembrane shedding cleavage site.Journal of thrombosis and haemostasis : JTH · 2013Article
- Adhesion maturation of neutrophils on nanoscopically presented platelet glycoprotein Ibα.ACS nano · 2013Article
- Identification of a calmodulin-binding domain in Sema4D that regulates its exodomain shedding in platelets.Blood · 2013Article
- Transmembrane domains are critical to the interaction between platelet glycoprotein V and glycoprotein Ib-IX complex.Journal of thrombosis and haemostasis : JTH · 2012Article
- Interaction of calmodulin with L-selectin at the membrane interface: implication on the regulation of L-selectin shedding.Journal of molecular biology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
Ectodomain shedding of transmembrane proteins may be regulated by their cytoplasmic domains. To date, the effecting cytoplasmic domain and the shed extracellular domain have been in the same polypeptide. In this study, shedding of GPIbα, the ligand-binding subunit of the platelet GPIb-IX complex and a marker for platelet senescence and storage lesion, was assessed in Chinese hamster ovary cells with/without functional GPIbα sheddase ADAM17. Mutagenesis of the GPIb-IX complex, which contains GPIbα, GPIbβ, and GPIX subunits, revealed that the intracellular membrane-proximal calmodulin-binding region of GPIbβ is critical for ADAM17-dependent shedding of GPIbα induced by the calmodulin inhibitor, W7. Perturbing the interaction between GPIbα and GPIbβ subunits further lessened the restraint of GPIbβ on GPIbα shedding. However, contrary to the widely accepted model of calmodulin regulation of ectodomain shedding, the R152E/L153E mutation in the GPIbβ cytoplasmic domain disrupted calmodulin binding to GPIbβ but had little effect on GPIbα shedding. Analysis of induction of GPIbα shedding by membrane-permeable GPIbβ-derived peptides implicated the association of GPIbβ with an unidentified intracellular protein in mediating regulation of GPIbα shedding. Overall, these results provide evidence for a novel trans-subunit mechanism for regulating ectodomain shedding.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.