ArticleMolecular biology of the cell2002
Role of secretory carrier membrane protein SCAMP2 in granule exocytosis.
Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.
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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.
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Who cites it
28 citing papers in PubMed, 1 synthesis or guideline pooled it, 55 citations in OpenAlex.
- Analysis of genetically determined gene expression suggests role of inflammatory processes in exfoliation syndrome.BMC genomics · 2023Pooled it
- Targeting SCAMP2 by a natural product auxarconjugatin B for glioblastoma therapyActa pharmaceutica Sinica. B · 2026Article
- Article
- Depalmitoylation and cell physiology: APT1 as a mediator of metabolic signals.American journal of physiology. Cell physiology · 2024Review
- Palmitoylation couples insulin hypersecretion with β cell failure in diabetes.Cell metabolism · 2023Article
- Secretory carrier-associated membrane protein 2 (SCAMP2) regulates cell surface expression of T-type calcium channels.Molecular brain · 2022Article
- SCAMP2/5 as diagnostic and prognostic markers for acute myeloid leukemia.Scientific reports · 2021Article
- SCAMP5 mediates activity-dependent enhancement of NHE6 recruitment to synaptic vesicles during synaptic plasticity.Molecular brain · 2021Article
- Article
- Anaphylactic Degranulation of Mast Cells: Focus on Compound Exocytosis.Journal of immunology research · 2019Review
- Post-Golgi Trafficking and Transport of Cell Wall Components.Frontiers in plant science · 2018Review
- Overexpression of SCAMP3 is an indicator of poor prognosis in hepatocellular carcinoma.Oncotarget · 2017Article
- Proteomic Profile of Brucella abortus-Infected Bovine Chorioallantoic Membrane Explants.PloS one · 2016Article
- SCAMP5 plays a critical role in synaptic vesicle endocytosis during high neuronal activity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Vesicular trafficking and signaling for cytokine and chemokine secretion in mast cells.Frontiers in immunology · 2014Review
- Secretory carrier membrane proteins.Protoplasma · 2012Review
- The secreted plant N-glycoproteome and associated secretory pathways.Frontiers in plant science · 2012Article
- The SNARE Machinery in Mast Cell Secretion.Frontiers in immunology · 2012Article
- Regulation of fusion pore closure and compound exocytosis in neuroendocrine PC12 cells by SCAMP1.Traffic (Copenhagen, Denmark) · 2011Article
- Secretory carrier membrane protein 2 regulates exocytic insertion of NKCC2 into the cell membrane.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
In secretory carrier membrane proteins (SCAMPs), the most conserved structural segment is between transmembrane spans 2 and 3, facing the cytosol. A synthetic peptide, CWYRPIYKAFR (E peptide), from this segment of SCAMP2 potently inhibits exocytosis in permeabilized neuroendocrine (PC12) cells. E peptide blocked discharge of (35)S-labeled secretogranin with the same structural selectivity and potency as observed for hexosaminidase secretion in mast cells. SCAMPs 1 and 2 are concentrated primarily on intracellular membranes in PC12 cells. Both, however, are found on plasma membranes, but neither is present on large dense-core vesicles. Yet, large dense-core vesicles marked by secretogranin attach to plasma membranes at foci containing SCAMP2 along with syntaxin1 and complexin at putative cell-surface docking/fusion sites. Regulated overexpression of SCAMP2 with point mutations in its E peptide but not of normal SCAMP2 caused dose-dependent inhibition of depolarization-induced secretion. The SCAMP2 mutants also inhibited secretion stimulated by elevated calcium. Inhibition was largely overcome by adding lysophosphatidylcholine to the medium at concentrations that do not otherwise affect secretion. Although overexpression of normal or mutant SCAMP2 slightly inhibits endocytosis, this effect does not appear to be related to the specific effect of the mutant SCAMP on stimulated exocytosis. Thus, SCAMP2 not only colocalizes with fusion sites but also appears to have an essential function in granule exocytosis through actions mediated by its E peptide-containing domain.
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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.