ArticleBlood2011
Residues within a lipid-associated segment of the PECAM-1 cytoplasmic domain are susceptible to inducible, sequential phosphorylation.
Article in Blood, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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.
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Who cites it
25 citing papers in PubMed.
- Charge-based immunoreceptor signalling in health and disease.Nature reviews. Immunology · 2025Review
- Regulation of lipid storage and inflammation in the liver by CEACAM1.European journal of clinical investigation · 2024Review
- CD31 as a probable responding and gate-keeping protein of the blood-brain barrier and the risk of Alzheimer's disease.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2023Review
- PIEZO1 and PECAM1 interact at cell-cell junctions and partner in endothelial force sensing.Communications biology · 2023Article
- Platelet dysfunction in platelet-type von Willebrand disease due to the constitutive triggering of the Lyn-PECAM1 inhibitory pathway.Haematologica · 2022Article
- The enigmatic nature of the triggering receptor expressed in myeloid cells -1 (TLT- 1).Platelets · 2021Review
- Hyperglycemia-induced ubiquitination and degradation of β-catenin with the loss of platelet endothelial cell adhesion molecule-1 in retinal endothelial cells.Microcirculation (New York, N.Y. : 1994) · 2020Article
- OsteoBLAST: Computational Routine of Global Molecular Analysis Applied to Biomaterials Development.Frontiers in bioengineering and biotechnology · 2020Article
- Negative regulators of platelet activation and adhesion.Journal of thrombosis and haemostasis : JTH · 2018Review
- CRISPR-mediated deletion of the PECAM-1 cytoplasmic domain increases receptor lateral mobility and strengthens endothelial cell junctional integrity.Life sciences · 2018Article
- Review
- Endothelial functions of platelet/endothelial cell adhesion molecule-1 (CD31).Current opinion in hematology · 2016Review
- Multisite Phosphorylation Modulates the T Cell Receptor ζ-Chain Potency but not the Switchlike Response.Biophysical journal · 2016Article
- The adhesion molecule PECAM-1 enhances the TGF-β-mediated inhibition of T cell function.Science signaling · 2016Article
- Juxtamembrane contribution to transmembrane signaling.Biopolymers · 2015Review
- Platelet Activation and Thrombus Formation over IgG Immune Complexes Requires Integrin αIIbβ3 and Lyn Kinase.PloS one · 2015Article
- Membrane-enabled dimerization of the intrinsically disordered cytoplasmic domain of ADAM10.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Regulation of endothelial cell barrier function by antibody-driven affinity modulation of platelet endothelial cell adhesion molecule-1 (PECAM-1).The Journal of biological chemistry · 2014Article
- PECAM-1: regulator of endothelial junctional integrity.Cell and tissue research · 2014Review
- Unreported intrinsic disorder in proteins: Building connections to the literature on IDPs.Intrinsically disordered proteins · 2014Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing receptors inhibit cellular responsiveness to immunoreceptor tyrosine-based activation motif (ITAM)-linked receptors. Although tyrosine phosphorylation is central to the initiation of both inhibitory ITIM and stimulatory ITAM signaling, the events that regulate receptor phosphorylation are incompletely understood. Previous studies have shown that ITAM tyrosines engage in structure-inducing interactions with the plasma membrane that must be relieved for phosphorylation to occur. Whether ITIM phosphorylation is similarly regulated and the mechanisms responsible for release from plasma membrane interactions to enable phosphorylation, however, have not been defined. PECAM-1 is a dual ITIM-containing receptor that inhibits ITAM-dependent responses in hematopoietic cells. We found that the PECAM-1 cytoplasmic domain is unstructured in an aqueous environment but adopts an α-helical conformation within a localized region on interaction with lipid vesicles that mimic the plasma membrane. The lipid-interacting segment contains the C-terminal ITIM tyrosine and a serine residue that undergo activation-dependent phosphorylation. The N-terminal ITIM is excluded from the lipid-interacting segment, and its phosphorylation is secondary to phosphorylation of the membrane-interacting C-terminal ITIM. On the basis of these findings, we propose a novel model for regulation of inhibitory signaling by ITIM-containing receptors that relies on reversible plasma membrane interactions and sequential ITIM phosphorylation.
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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.