ArticleMolecular biology of the cell1992
Cytoplasmic domain of P-selectin (CD62) contains the signal for sorting into the regulated secretory pathway.
Article in Molecular biology of the cell, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 154 citations in OpenAlex.
- Pathological P-Selectin Upregulation Promotes Retinal Ganglion Cell Degeneration Accompanied by T-Cell Recruitment in Glaucoma.Investigative ophthalmology & visual science · 2026Article
- Characterization of complement C3 as a marker of alpha-amanitin toxicity by comparative secretome profiling.Toxicological research · 2023Article
- Sorting nexin 24 is required for α-granule biogenesis and cargo delivery in megakaryocytes.Haematologica · 2022Article
- Targeting transgenic proteins to alpha granules for platelet-directed gene therapy.Molecular therapy. Nucleic acids · 2022Article
- Syntaxin 12 and COMMD3 are new factors that function with VPS33B in the biogenesis of platelet α-granules.Blood · 2022Article
- The life cycle of platelet granules.F1000Research · 2018Review
- Protein mobilities and P-selectin storage in Weibel-Palade bodies.Journal of cell science · 2010Article
- Platelet alpha-granules: basic biology and clinical correlates.Blood reviews · 2009Review
- Article
- Phenotypic heterogeneity in the Gray platelet syndrome extends to the expression of TREM family member, TLT-1.Thrombosis and haemostasis · 2008Article
- Sorting nexin 17 accelerates internalization yet retards degradation of P-selectin.Molecular biology of the cell · 2004Article
- Peritoneal macrophages express both P-selectin and PSGL-1.The Journal of cell biology · 2003Article
- Defect in regulated secretion of P-selectin affects leukocyte recruitment in von Willebrand factor-deficient mice.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Rapid transport of internalized P-selectin to late endosomes and the TGN: roles in regulating cell surface expression and recycling to secretory granules.The Journal of cell biology · 2000Article
- A complex web of signal-dependent trafficking underlies the triorganellar distribution of P-selectin in neuroendocrine PC12 cells.The Journal of cell biology · 1999Article
- Role of P-selectin cytoplasmic domain in granular targeting in vivo and in early inflammatory responses.The Journal of cell biology · 1998Article
- Determinants in the cytoplasmic domain of P-selectin required for sorting to secretory granules.The Biochemical journal · 1998Article
- P-Selectin: Basic Aspects.Journal of thrombosis and thrombolysis · 1998Article
- Interactions of the cytoplasmic domain of P-selectin with clathrin-coated pits enhance leukocyte adhesion under flow.The Journal of cell biology · 1998Article
- An atypical sorting determinant in the cytoplasmic domain of P-selectin mediates endosomal sorting.Molecular biology of the cell · 1998Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
P-selectin (CD62), formerly called GMP-140 or PADGEM, is a membrane protein located in secretory storage granules of platelets and endothelial cells. To study the mechanisms responsible for the targeting of P-selectin to storage granules, we transfected its cDNA into COS-7 and CHO-K1 cells, which lack a regulated exocytic pathway, or into AtT20 cells, which are capable of regulated secretion. P-selectin was expressed on the plasma membrane of COS-7 and CHO-K1 cells but was concentrated in storage granules of AtT20 cells. Immunogold electron microscopy indicated that the electron-dense granules containing P-selectin in AtT20 cells also stored the endogenous soluble hormone ACTH. Activation of AtT20 cells with 8-Br-cAMP increased the surface expression of P-selectin, consistent with agonist-induced fusion of granule membranes with the plasma membrane. Deletion of the last 23 amino acids of the 35-residue cytoplasmic domain resulted in delivery of P-selectin to the plasma membrane of AtT20 cells. Replacement of the cytoplasmic tail of tissue factor, a plasma membrane protein, with the cytoplasmic domain of P-selectin redirected the chimeric molecule to granules. We conclude that the cytoplasmic domain of P-selectin is both necessary and sufficient for sorting of membrane proteins into the regulated pathway of secretion.
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