Evidence map›Paper›PMID 7876313›Full record

ArticleThe Journal of cell biology1995

Dephosphorylated synapsin I anchors synaptic vesicles to actin cytoskeleton: an analysis by videomicroscopy.

P E Ceccaldi, F Grohovaz, F Benfenati, E Chieregatti, P Greengard, F Valtorta

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.2field-weighted citation impact, top 4% 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

51 citing papers in PubMed, 162 citations in OpenAlex.

  1. Review
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  7. The Phosphoprotein Synapsin Ia Regulates the Kinetics of Dense-Core Vesicle Release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  8. Article
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  10. Review
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  12. Review
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  15. Article
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  17. Article
  18. Multiple roles for the actin cytoskeleton during regulated exocytosis.Cellular and molecular life sciences : CMLS · 2013
    Review
  19. Synapsins contribute to the dynamic spatial organization of synaptic vesicles in an activity-dependent manner.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
  20. Piccolo regulates the dynamic assembly of presynaptic F-actin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011
    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

6 authors at 1 institution in 1 country.

P E CeccaldiB. Ceccarelli Center, Department of Medical Pharmacology, DIBIT S. Raffaele Scientific Institute, Milano, Italy.
F Grohovaz
F Benfenati
E Chieregatti
P Greengard
F Valtorta
Vita-Salute San Raffaele University · IT

Funding

SYNAPSINS: REGULATORS OF NEUROTRANSMITTER RELEASER01MH039327 · NIMH · ROCKEFELLER UNIVERSITY · PI GREENGARD, PAUL · 1985 to 2006
$2.9M
SYNAPSINS: REGULATORS OF NEUROTRANSMITTER RELEASER37MH039327 · NIMH · ROCKEFELLER UNIVERSITY · PI GREENGARD, PAUL · 1991 to 2000
$671k
NIMH NIH HHS MH 39327Telethon 581
6 · The paper itself

Abstract

Synapsin I is a synaptic vesicle-associated protein which inhibits neurotransmitter release, an effect which is abolished upon its phosphorylation by Ca2+/calmodulin-dependent protein kinase II (CaM kinase II). Based on indirect evidence, it was suggested that this effect on neurotransmitter release may be achieved by the reversible anchoring of synaptic vesicles to the actin cytoskeleton of the nerve terminal. Using video-enhanced microscopy, we have now obtained experimental evidence in support of this model: the presence of dephosphorylated synapsin I is necessary for synaptic vesicles to bind actin; synapsin I is able to promote actin polymerization and bundling of actin filaments in the presence of synaptic vesicles; the ability to cross-link synaptic vesicles and actin is specific for synapsin I and is not shared by other basic proteins; the cross-linking between synaptic vesicles and actin is specific for the membrane of synaptic vesicles and does not reflect either a non-specific binding of membranes to the highly surface active synapsin I molecule or trapping of vesicles within the thick bundles of actin filaments; the formation of the ternary complex is virtually abolished when synapsin I is phosphorylated by CaM kinase II. The data indicate that synapsin I markedly affects synaptic vesicle traffic and cytoskeleton assembly in the nerve terminal and provide a molecular basis for the ability of synapsin I to regulate the availability of synaptic vesicles for exocytosis and thereby the efficiency of neurotransmitter release.

Indexed as

ActinsAnimalsCattleCytoskeletonEnergy TransferMicroscopy, FluorescenceMicroscopy, VideoPhosphorylationProsencephalonProtein BindingRabbitsRatsSynapsinsSynaptic VesiclesActinsSynapsins

Identifiers

PMID7876313
PMCPMC2120389
OpenAlexW2123557321

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.