Evidence map›Paper›PMID 21041449›Full record

ArticleThe Journal of cell biology2010

Palmitoylation-dependent association with CD63 targets the Ca2+ sensor synaptotagmin VII to lysosomes.

Andrew R Flannery, Cecilia Czibener, Norma W Andrews

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

47 citing papers in PubMed, 78 citations in OpenAlex.

  1. Alternative splicing of synaptotagmin 7 regulates oligomerization and short-term synaptic plasticity.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Revisiting the role of Annexins in membrane trafficking.Cellular and molecular life sciences : CMLS · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Exocytosis of Nanoparticles: A Comprehensive Review.Nanomaterials (Basel, Switzerland) · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Function of Drosophila Synaptotagmins in membrane trafficking at synapses.Cellular and molecular life sciences : CMLS · 2021
    Review
  20. Review
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

3 authors at 3 institutions in 2 countries.

Andrew R FlanneryDepartment of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742, USA.
Cecilia Czibener
Norma W Andrews
Consejo Nacional de Investigaciones Científicas y Técnicas · ARUniversity of Maryland, College Park · USYale University · US

Funding

Regulated exocytosis of lysosomes and plasma membrane repairR01GM064625 · NIGMS · YALE UNIVERSITY · PI ANDREWS, NORMA WINDSOR, SONG, WENXIA · 2002 to 2020
$6.3M
Molecular interactions involved in calcium-regulated phagocytosisF32GM082145 · NIGMS · YALE UNIVERSITY · PI FLANNERY, ANDREW · 2007 to 2009
$154k
NIGMS NIH HHS F32 GM082145NIGMS NIH HHS R01 GM064625
6 · The paper itself

Abstract

Syt VII is a Ca(2+) sensor that regulates lysosome exocytosis and plasma membrane repair. Because it lacks motifs that mediate lysosomal targeting, it is unclear how Syt VII traffics to these organelles. In this paper, we show that mutations or inhibitors that abolish palmitoylation disrupt Syt VII targeting to lysosomes, causing its retention in the Golgi complex. In macrophages, Syt VII is translocated simultaneously with the lysosomal tetraspanin CD63 from tubular lysosomes to nascent phagosomes in a Ca(2+)-dependent process that facilitates particle uptake. Mutations in Syt VII palmitoylation sites block trafficking of Syt VII, but not CD63, to lysosomes and phagosomes, whereas tyrosine replacement in the lysosomal targeting motif of CD63 causes both proteins to accumulate on the plasma membrane. Complexes of CD63 and Syt VII are detected only when Syt VII palmitoylation sites are intact. These findings identify palmitoylation-dependent association with the tetraspanin CD63 as the mechanism by which Syt VII is targeted to lysosomes.

Indexed as

AnimalsAntigens, CDCalciumCells, CulturedLipoylationLysosomesMiceMice, Inbred C57BLMice, KnockoutPlatelet Membrane GlycoproteinsSynaptotagminsTetraspanin 30Antigens, CDCalciumCd63 protein, mousePlatelet Membrane GlycoproteinsSynaptotagminsSyt7 protein, mouseTetraspanin 30

Identifiers

PMID21041449
PMCPMC3003310
OpenAlexW2044414150

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.