Evidence map›Paper›PMID 29794152›Full record

ReviewThe Journal of general physiology2018

The high-affinity calcium sensor synaptotagmin-7 serves multiple roles in regulated exocytosis.

Daniel D MacDougall, Zesen Lin, Nara L Chon, Skyler L Jackman, Hai Lin, Jefferson D Knight, Arun Anantharam

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of general physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

37 citing papers in PubMed, 68 citations in OpenAlex.

  1. Increased CA3 burst activity inbioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Exosome: an overview on enhanced biogenesis by small molecules.Naunyn-Schmiedeberg's archives of pharmacology · 2025
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Synaptotagmin 7 Sculpts Short-Term Plasticity at a High Probability Synapse.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  13. Article
  14. Review
  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

7 authors at 3 institutions in 1 country.

Daniel D MacDougallDepartment of Pharmacology, University of Michigan, Ann Arbor, MI.
Zesen LinDepartment of Pharmacology, University of Michigan, Ann Arbor, MI.
Nara L ChonDepartment of Chemistry, University of Colorado, Denver, CO.
Skyler L JackmanVollum Institute, Oregon Health & Science University, Portland, OR.ORCID 0000-0002-6500-3937
Hai LinDepartment of Chemistry, University of Colorado, Denver, CO.
Jefferson D KnightDepartment of Chemistry, University of Colorado, Denver, CO.ORCID 0000-0003-2208-4420
Arun AnantharamDepartment of Pharmacology, University of Michigan, Ann Arbor, MI.ORCID 0000-0001-8560-6180
University of Colorado Denver · USUniversity of Michigan · USOregon Health & Science University · US

Funding

The Impact of Synaptotagmin Isoform Structure and Diversity on Dense Core Granule ExocytosisR01GM111997 · NIGMS · WAYNE STATE UNIVERSITY · PI ANANTHARAM, ARUN · 2015 to 2019
$1.5M
Molecular Mechanisms of Protein-Membrane Interactions Driving Insulin SecretionR15GM102866 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI KNIGHT, JEFFERSON D. · 2014 to 2018
$871k
NIGMS NIH HHS R01 GM111997NIGMS NIH HHS R15 GM102866
6 · The paper itself

Abstract

Synaptotagmin (Syt) proteins comprise a 17-member family, many of which trigger exocytosis in response to calcium. Historically, most studies have focused on the isoform Syt-1, which serves as the primary calcium sensor in synchronous neurotransmitter release. Recently, Syt-7 has become a topic of broad interest because of its extreme calcium sensitivity and diversity of roles in a wide range of cell types. Here, we review the known and emerging roles of Syt-7 in various contexts and stress the importance of its actions. Unique functions of Syt-7 are discussed in light of recent imaging, electrophysiological, and computational studies. Particular emphasis is placed on Syt-7-dependent regulation of synaptic transmission and neuroendocrine cell secretion. Finally, based on biochemical and structural data, we propose a mechanism to link Syt-7's role in membrane fusion with its role in subsequent fusion pore expansion via strong calcium-dependent phospholipid binding.

Indexed as

ExocytosisAnimalsCalciumHumansMembrane FusionSecretory VesiclesSynaptotagminsCalciumSynaptotagmins

Identifiers

PMID29794152
PMCPMC5987875
OpenAlexW2803294422

What Socratic 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 Socratic graph.