Evidence map›Paper›PMID 11171079›Full record

ArticleThe Biochemical journal2001

Identification of synapsin I peptides that insert into lipid membranes.

J J Cheetham, S Hilfiker, F Benfenati, T Weber, P Greengard, A J Czernik

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

23 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Phase separation at the synapse.Nature neuroscience · 2020
    Review
  8. Article
  9. SIV-Mediated Synaptic Dysfunction Is Associated with an Increase in Synapsin Site 1 Phosphorylation and Impaired PP2A Activity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
  10. Article
  11. Synapsin Isoforms Regulating GABA Release from Hippocampal Interneurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016
    Article
  12. Review
  13. Functional role of ATP binding to synapsin I in synaptic vesicle trafficking and release dynamics.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  14. Fast vesicle transport is required for the slow axonal transport of synapsin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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
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 2 institutions in 2 countries.

J J CheethamLaboratory of Molecular and Cellular Neuroscience, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
S Hilfiker
F Benfenati
T Weber
P Greengard
A J Czernik
Rockefeller University · USUniversity of Genoa · IT

Funding

SYNAPSINS: REGULATORS OF NEUROTRANSMITTER RELEASER01MH039327 · NIMH · ROCKEFELLER UNIVERSITY · PI GREENGARD, PAUL · 1985 to 2006
$2.9M
SYNAPSINS, SYNAPTOGENESIS AND ALZHEIMERS DISEASEP01AG015072 · NIA · ROCKEFELLER UNIVERSITY · PI GREENGARD, PAUL · 1998 to 2002
$2.8M
SYNAPSINS: REGULATORS OF NEUROTRANSMITTER RELEASER37MH039327 · NIMH · ROCKEFELLER UNIVERSITY · PI GREENGARD, PAUL · 1991 to 2000
$671k
NIA NIH HHS AG 15072NIMH NIH HHS MH 39327Telethon 1131
6 · The paper itself

Abstract

The synapsins constitute a family of synaptic vesicle-associated phosphoproteins essential for regulating neurotransmitter release and synaptogenesis. The molecular mechanisms underlying the selective targeting of synapsin I to synaptic vesicles are thought to involve specific protein-protein interactions, while the high-affinity binding to the synaptic vesicle membrane may involve both protein-protein and protein-lipid interactions. The highly hydrophobic N-terminal region of the protein has been shown to bind with high affinity to the acidic phospholipids phosphatidylserine and phosphatidylinositol and to penetrate the hydrophobic core of the lipid bilayer. To precisely identify the domains of synapsin I which mediate the interaction with lipids, synapsin I was bound to liposomes containing the membrane-directed carbene-generating reagent 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine and subjected to photolysis. Isolation and N-terminal amino acid sequencing of 125I-labelled synapsin I peptides derived from CNBr cleavage indicated that three distinct regions in the highly conserved domain C of synapsin I insert into the hydrophobic core of the phospholipid bilayer. The boundaries of the regions encompass residues 166-192, 233-258 and 278-327 of bovine synapsin I. These regions are surface-exposed in the crystal structure of domain C of bovine synapsin I and are evolutionarily conserved among isoforms across species. The present data offer a molecular explanation for the high-affinity binding of synapsin I to phospholipid bilayers and synaptic vesicles.

Indexed as

Lipid BilayersAmino Acid SequenceAnimalsCattleEvolution, MolecularLiposomesModels, MolecularMolecular Sequence DataPeptide FragmentsPhospholipidsProtein ConformationSequence Homology, Amino AcidSynapsinsLipid BilayersLiposomesPeptide FragmentsPhospholipidsSynapsins

Identifiers

PMID11171079
PMCPMC1221628
OpenAlexW1968396722

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.