Evidence map›Paper›PMID 2497104›Full record

ArticleThe Journal of cell biology1989

Characterization of synapsin I fragments produced by cysteine-specific cleavage: a study of their interactions with F-actin.

M Bähler, F Benfenati, F Valtorta, A J Czernik, P Greengard

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

33 citing papers in PubMed, 117 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. A tris (2-carboxyethyl) phosphine (TCEP) related cleavage on cysteine-containing proteins.Journal of the American Society for Mass Spectrometry · 2010
    Article
  11. Structural domains involved in the regulation of transmitter release by synapsins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005
    Article
  12. Article
  13. Article
  14. Synapsin III: developmental expression, subcellular localization, and role in axon formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000
    Article
  15. Synapsins as regulators of neurotransmitter release.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 1999
    Review
  16. Article
  17. Synapsin I interacts with c-Src and stimulates its tyrosine kinase activity.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  18. 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.

M BählerLaboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York 10021.
F Benfenati
F Valtorta
A J Czernik
P Greengard
Rockefeller University · US

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
PROTEIN III AND ALCOHOLISMR01AA006944 · NIAAA · ROCKEFELLER UNIVERSITY · PI GREENGARD, PAUL · 1986 to 1989
–
EAPO CDC HHS EPA-CR813826NIAAA NIH HHS AA-06944NIMH NIH HHS MH-39327
6 · The paper itself

Abstract

Synapsin I is a neuron-specific phosphoprotein that is concentrated in the presynaptic nerve terminal in association with the cytoplasmic surface of synaptic vesicles. It has been demonstrated to bundle F-actin in a phosphorylation-dependent manner in vitro, a property consistent with its proposed role in linking synaptic vesicles to the cytoskeleton and its involvement in the regulation of neurotransmitter release. Synapsin I is composed of two distinct domains, a COOH terminal, collagenase-sensitive, hydrophilic, and strongly basic tail region, and an NH2 terminal, collagenase-resistant head region relatively rich in hydrophobic amino acids. To elucidate the structural basis for the interactions between synapsin I and F-actin and how it relates to other characteristics of synapsin I, we have performed a structure-function analysis of fragments of synapsin I produced by cysteine-specific cleavage with 2-nitro-5-thiocyanobenzoic acid. The fragments were identified and aligned with the parent molecule using the deduced primary structure of synapsin I and the known phosphorylation sites as markers. We have purified these fragments and examined their interactions with F-actin. Two distinct fragments, a 29-kD NH2-terminal fragment and a 15-kD middle fragment, were shown to contain F-actin binding sites. A 51/54-kD middle/tail fragment retained the F-actin binding and bundling activity of synapsin I, but the isolated tail fragment did not retain either activity. In contrast to phosphorylation of sites two and three in intact synapsin I, which abolishes F-actin bundling activity, phosphorylation of these sites in the middle/tail fragment failed to abolish this activity. In conclusion, three domains of synapsin I appear to be involved in F-actin binding and bundling.

Indexed as

ActinsAnimalsBrainCattleCysteineKineticsMicroscopy, ElectronMolecular WeightNerve Tissue ProteinsPeptide FragmentsPeptide MappingPhosphoproteinsPhosphorylationProtein BindingRabbitsSynapsinsActinsCysteineNerve Tissue ProteinsPeptide FragmentsPhosphoproteinsSynapsins

Identifiers

PMID2497104
PMCPMC2115537
OpenAlexW2070171796

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.