Evidence map›Paper›PMID 12475951›Full record

ArticleMolecular biology of the cell2002

Role of secretory carrier membrane protein SCAMP2 in granule exocytosis.

Lixia Liu, Zhenheng Guo, Quyen Tieu, Anna Castle, David Castle

Open access · greenAbstract read
In one paragraph

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.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
0.7field-weighted citation impact, top 33% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed, 1 synthesis or guideline pooled it, 55 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Depalmitoylation and cell physiology: APT1 as a mediator of metabolic signals.American journal of physiology. Cell physiology · 2024
    Review
  5. Article
  6. Article
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  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. 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 · 2014
    Article
  15. Review
  16. Review
  17. Article
  18. The SNARE Machinery in Mast Cell Secretion.Frontiers in immunology · 2012
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Lixia LiuDepartment of Cell Biology, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908-0001, USA.
Zhenheng Guo
Quyen Tieu
Anna Castle
David Castle
University of Virginia · US

Funding

MEMBRANE FUNCTION IN PAROTID SECRETORY MECHANISMSR01DE009655 · NIDCR · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI CASTLE, JOHN DAVID · 1991 to 2005
$2.0M
NIDCR NIH HHS DE-09655NIDCR NIH HHS R01 DE009655
6 · The paper itself

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.

Indexed as

Adaptor Proteins, Vesicular TransportAnimalsAntigens, SurfaceCalciumCarrier ProteinsCell MembraneCloning, MolecularDNA, ComplementaryDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelExocytosisIonophoresMembrane ProteinsMutagenesis, Site-DirectedMutationNerve Tissue ProteinsAdaptor Proteins, Vesicular TransportAntigens, SurfaceCalciumCarrier Proteinscomplexin IDNA, ComplementaryIonophoresMembrane ProteinsNerve Tissue ProteinsPeptidesPhorbol EstersSCAMP2 protein, humanSyntaxin 1TetracyclineTransferrin

Identifiers

PMID12475951
PMCPMC138632
OpenAlexW2125755426

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.