Evidence map›Paper›PMID 21272170›Full record

ArticleTraffic (Copenhagen, Denmark)2011

Regulation of fusion pore closure and compound exocytosis in neuroendocrine PC12 cells by SCAMP1.

Jie Zhang, David Castle

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Depalmitoylation and cell physiology: APT1 as a mediator of metabolic signals.American journal of physiology. Cell physiology · 2024
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. 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
  10. Article
  11. Multiple roles for the actin cytoskeleton during regulated exocytosis.Cellular and molecular life sciences : CMLS · 2013
    Review
  12. Article
  13. Review
  14. 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

2 authors at 1 institution in 1 country.

Jie ZhangDepartment of Cell Biology, Molecular, Cell and Developmental Biology Program, University of Virginia, Charlottesville, VA 22908-0732, USA. jz5p@virginia.edu
David Castle
University of Virginia · US

Funding

Exocytosis and Coupled Endocytosis in Neuroendocrine CellsR01DK073380 · NIDDK · UNIVERSITY OF VIRGINIA · PI CASTLE, JOHN DAVID · 2006 to 2010
$1.5M
NIDDK NIH HHS DK073380NIDDK NIH HHS R01 DK073380
6 · The paper itself

Abstract

During exocytosis, neuroendocrine cells can achieve partial release of stored secretory products from dense core vesicles (DCVs) by coupling endocytosis directly at fusion sites and without full discharge. The physiological role of partial secretion is of substantial interest. Much is known about SNARE-mediated initiation of exocytosis and dynamin-mediated completion of endocytosis, but little is known about coupling events. We have used real-time microscopy to examine the role of secretory carrier membrane protein SCAMP1 in exo-endocytic coupling in PC12 cells. While reduced SCAMP1 expression is known to impede dilation of newly opened fusion pores during onset of DCV exocytosis, we now show that SCAMP1 deficiency also inhibits closure of fusion pores after they have opened. Inhibition causes accumulation of fusion figures at the plasma membrane. Closure is recovered by restoring expression and accelerated slightly by overexpression. Interestingly, inhibited pore closure resulting from loss of SCAMP1 appears to increase secondary fusion of DCVs to already-fused DCVs (compound exocytosis). Unexpectedly, reinternalization of expanded DCV membranes following compound exocytosis appears to proceed normally in SCAMP1-deficient cells. SCAMP1's apparent dual role in facilitating dilation and closure of fusion pores implicates its function in exo-endocytic coupling and in the regulation of partial secretion. Secondarily, SCAMP1 may serve to limit the extent of compound exocytosis.

Indexed as

AnimalsCalciumCarrier ProteinsCell MembraneEndocytosisExocytosisIntracellular Signaling Peptides and ProteinsMembrane FusionMembrane ProteinsPC12 CellsRatsRNA, Small InterferingCalciumCarrier ProteinsIntracellular Signaling Peptides and ProteinsMembrane ProteinsRNA, Small InterferingScamp1 protein, rat

Identifiers

PMID21272170
PMCPMC3085939
OpenAlexW2066058305

What OpenQuestion holds

Textmetadata
LicenceTDM
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.