Evidence map›Paper›PMID 2497106›Full record

ArticleThe Journal of cell biology1989

Interactions of synapsin I with small synaptic vesicles: distinct sites in synapsin I bind to vesicle phospholipids and vesicle proteins.

F Benfenati, M Bähler, R Jahn, 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 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
6.5field-weighted citation impact, top 2% 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

63 citing papers in PubMed, 186 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Synapsin Is Required for Dense Core Vesicle Capture and cAMP-Dependent Neuropeptide Release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  9. Review
  10. Article
  11. Phase separation at the synapse.Nature neuroscience · 2020
    Review
  12. Article
  13. Article
  14. Article
  15. A liquid phase of synapsin and lipid vesicles.Science (New York, N.Y.) · 2018
    Article
  16. Review
  17. Octopaminergic innervation and a neurohaemal release site in the antennal heart of the locust Schistocerca gregaria.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2018
    Article
  18. Article
  19. Article
  20. Article

3 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

F BenfenatiLaboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York 10021.
M Bähler
R Jahn
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
NEUROPEPTIDE EFFECTS ON BRAIN PROTEIN PHOSPHORYLATIONF05TW003645 · FIC · ROCKEFELLER UNIVERSITY · PI BENFENATI, FABIO · 1985 to 1987
–
PROTEIN III AND ALCOHOLISMR01AA006944 · NIAAA · ROCKEFELLER UNIVERSITY · PI GREENGARD, PAUL · 1986 to 1989
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FIC NIH HHS 1 F05 TW03645-01 BI-5 AHRNIAAA NIH HHS AA-06944NIMH NIH HHS MH-39327
6 · The paper itself

Abstract

Synapsin I is a major neuron-specific phosphoprotein that is specifically localized to the cytoplasmic surface of small synaptic vesicles. In the present study, the binding of synapsin I to small synaptic vesicles was characterized in detail. The binding of synapsin I was preserved when synaptic vesicles were solubilized and reconstituted in phosphatidylcholine. After separation of the protein and lipid components of synaptic vesicles under nondenaturing conditions, synapsin I bound to both components. The use of hydrophobic labeling procedures allowed the assessment of interactions between phospholipids and synapsin I in intact synaptic vesicles. Hydrophobic photolabeling followed by cysteine-specific cleavage of synapsin I demonstrated that the head domain of synapsin I penetrates into the hydrophobic core of the bilayer. The purified NH2-terminal fragment, derived from the head domain by cysteine-specific cleavage, bound to synaptic vesicles with high affinity confirming the results obtained from hydrophobic photolabeling. Synapsin I binding to synaptic vesicles could be inhibited by the entire molecule or by the combined presence of the NH2-terminal and tail fragments, but not by an excess of either NH2-terminal or tail fragment alone. The purified tail fragment bound with relatively high affinity to synaptic vesicles, though it did not significantly interact with phospholipids. Binding of the tail fragment was competed by holosynapsin I; was greatly decreased by phosphorylation; and was abolished by high ionic strength conditions or protease treatment of synaptic vesicles. The data suggest the existence of two sites of interaction between synapsin I and small synaptic vesicles: binding of the head domain to vesicle phospholipids and of the tail domain to a protein component of the vesicle membrane. The latter interaction is apparently responsible for the salt and phosphorylation dependency of synapsin I binding to small synaptic vesicles.

Indexed as

AnimalsBinding SitesBrainCattleKineticsLipid BilayersNerve Tissue ProteinsPeptide FragmentsPhospholipidsPhosphoproteinsProtein BindingSynapsinsSynaptic VesiclesLipid BilayersNerve Tissue ProteinsPeptide FragmentsPhospholipidsPhosphoproteinsSynapsins

Identifiers

PMID2497106
PMCPMC2115532
OpenAlexW2146947437

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.