Evidence map›Paper›PMID 29127297›Full record

ArticleScientific reports2017

Rab5 is critical for SNAP23 regulated granule-granule fusion during compound exocytosis.

Ofir Klein, Amit Roded, Neta Zur, Nurit P Azouz, Olga Pasternak, Koret Hirschberg, Ilan Hammel, Paul A Roche, Ayaka Yatsu, Mitsunori Fukuda and 2 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. LRO biogenesis and function: what can we learn from mast cells?Frontiers in cell and developmental biology · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Endosomal Rab GTPases regulate secretory granule maturation inCommunicative & integrative biology · 2021
    Article
  9. Review
  10. Review
  11. MHC class I and II peptide homology regulates the cellular immune response.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Imaging FITC-dextran as a Reporter for Regulated Exocytosis.Journal of visualized experiments : JoVE · 2018
    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

12 authors at 5 institutions in 3 countries.

Ofir KleinDepartment of Cell and Developmental Biology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, 69978, Israel.
Amit RodedDepartment of Cell and Developmental Biology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, 69978, Israel.
Neta ZurDepartment of Cell and Developmental Biology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, 69978, Israel.
Nurit P AzouzDepartment of Cell and Developmental Biology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, 69978, Israel.
Olga PasternakDepartment of Cell and Developmental Biology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, 69978, Israel.
Koret HirschbergDepartment of Pathology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, 69978, Israel.
Ilan HammelDepartment of Pathology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, 69978, Israel.
Paul A RocheExperimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, 20892, USA.
Ayaka YatsuLaboratory of Membrane Trafficking Mechanisms, Department of Developmental Biology and Neurosciences, Graduate School of Life Sciences, Tohoku University, Aobayama, Aoba-ku, Sendai, Miyagi, 980-8578, Japan.
Mitsunori FukudaLaboratory of Membrane Trafficking Mechanisms, Department of Developmental Biology and Neurosciences, Graduate School of Life Sciences, Tohoku University, Aobayama, Aoba-ku, Sendai, Miyagi, 980-8578, Japan.ORCID 0000-0002-8620-5853
Stephen J GalliDepartments of Pathology and of Microbiology and Immunology, and Sean N. Parker Center for Allergy and Asthma Research, Stanford University School of Medicine, Stanford, California, 94305-5176, USA.
Ronit Sagi-EisenbergDepartment of Cell and Developmental Biology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, 69978, Israel. histol3@post.tau.ac.il.
Tel Aviv University · ILTohoku University · JPCincinnati Children's Hospital Medical Center · USNational Institutes of Health · USStanford University · US

Funding

Tracking allergen specific T cells in multi-food allergyU19AI104209 · NIAID · STANFORD UNIVERSITY · PI GALLI, STEPHEN JOSEPH · 2013 to 2025
$17.3M
Mechanisms of MHC Class II Association with Plasma Membrane MicrodomainsZIABC011033 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI ROCHE, PAUL · 2009 to 2020
$3.4M
RabGEF1 in MyD88 signaling, skin immunity, and atopic dermatitisR01AR067145 · NIAMS · STANFORD UNIVERSITY · PI GALLI, STEPHEN JOSEPH · 2015 to 2019
$1.9M
NIAID NIH HHS U19 AI104209NIAMS NIH HHS R01 AR067145
6 · The paper itself

Abstract

Compound exocytosis is considered the most massive mode of exocytosis, during which the membranes of secretory granules (SGs) fuse with each other to form a channel through which the entire contents of their granules is released. The underlying mechanisms of compound exocytosis remain largely unresolved. Here we show that the small GTPase Rab5, a known regulator of endocytosis, is pivotal for compound exocytosis in mast cells. Silencing of Rab5 shifts receptor-triggered secretion from a compound to a full exocytosis mode, in which SGs individually fuse with the plasma membrane. Moreover, we show that Rab5 is essential for FcεRI-triggered association of the SNARE protein SNAP23 with the SGs. Direct evidence is provided for SNAP23 involvement in homotypic SG fusion that occurs in the activated cells. Finally, we show that this fusion event is prevented by inhibition of the IKKβ2 kinase, however, neither a phosphorylation-deficient nor a phosphomimetic mutant of SNAP23 can mediate homotypic SG fusion in triggered cells. Taken together our findings identify Rab5 as a heretofore-unrecognized regulator of compound exocytosis that is essential for SNAP23-mediated granule-granule fusion. Our results also implicate phosphorylation cycles in controlling SNAP23 SNARE function in homotypic SG fusion.

Indexed as

Cell LineCell MembraneExocytosisHumansMembrane FusionPhosphorylationQb-SNARE ProteinsQc-SNARE Proteinsrab5 GTP-Binding ProteinsSecretory VesiclesQb-SNARE ProteinsQc-SNARE ProteinsRAB5C protein, humanrab5 GTP-Binding ProteinsSNAP23 protein, human

Identifiers

PMID29127297
PMCPMC5681557
OpenAlexW2767313824

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.