Evidence map›Paper›PMID 21928778›Full record

ArticleBiochemistry2011

Post-translational modifications and lipid binding profile of insect cell-expressed full-length mammalian synaptotagmin 1.

Marija Vrljic, Pavel Strop, Ryan C Hill, Kirk C Hansen, Steven Chu, Axel T Brunger

Open access · bronzeAbstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

22 citing papers in PubMed, 29 citations in OpenAlex.

  1. The Core Complex of the CaJournal of molecular biology · 2023
    Review
  2. Calcium Sensors of Neurotransmitter Release.Advances in neurobiology · 2023
    Article
  3. Review
  4. Article
  5. Gangliosides interact with synaptotagmin to form the high-affinity receptor complex for botulinum neurotoxin B.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Gasotransmitter Heterocellular Signaling.Antioxidants & redox signaling · 2017
    Article
  11. Article
  12. PtdInsPeLife · 2016
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. 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

6 authors at 5 institutions in 1 country.

Marija VrljicDepartment of Molecular and Cellular Physiology, Stanford University, Stanford, California 94305-5432, USA.
Pavel Strop
Ryan C Hill
Kirk C Hansen
Steven Chu
Axel T Brunger
Howard Hughes Medical Institute · USLawrence Berkeley National Laboratory · USStanford University · USUniversity of Colorado Anschutz Medical Campus · USUniversity of Colorado Health · US

Funding

Single molecule studies of SNARE-induced vesicle fusionR37MH063105 · NIMH · STANFORD UNIVERSITY · PI BRUNGER, AXEL T · 2011 to 2020
$4.7M
Howard Hughes Medical InstituteNIMH NIH HHS R37 MH063105NIMH NIH HHS R37-MH63105
6 · The paper itself

Abstract

Synaptotagmin 1 (Syt1) is a Ca(2+) sensor for SNARE-mediated, Ca(2+)-triggered synaptic vesicle fusion in neurons. It is composed of luminal, transmembrane, linker, and two Ca(2+)-binding (C2) domains. Here we describe expression and purification of full-length mammalian Syt1 in insect cells along with an extensive biochemical characterization of the purified protein. The expressed and purified protein is properly folded and has increased α-helical content compared to the C2AB fragment alone. Post-translational modifications of Syt1 were analyzed by mass spectrometry, revealing the same modifications of Syt1 that were previously described for Syt1 purified from brain extract or mammalian cell lines, along with a novel modification of Syt1, tyrosine nitration. A lipid binding screen with both full-length Syt1 and the C2AB fragments of Syt1 and Syt3 isoforms revealed new Syt1-lipid interactions. These results suggest a conserved lipid binding mechanism in which Ca(2+)-independent interactions are mediated via a lysine rich region of the C2B domain while Ca(2+)-dependent interactions are mediated via the Ca(2+)-binding loops.

Indexed as

Lipid MetabolismProtein Processing, Post-TranslationalAmino Acid SequenceAnimalsCell LineCloning, MolecularGene ExpressionGlycosylationInsectaModels, MolecularMolecular Sequence DataPhosphorylationProtein BindingProtein FoldingProtein Structure, SecondaryRatsSynaptotagmin I

Identifiers

PMID21928778
PMCPMC3217305
OpenAlexW2052023774

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.