Evidence map›Paper›PMID 16052212›Full record

ArticleThe EMBO journal2005

A Munc13/RIM/Rab3 tripartite complex: from priming to plasticity?

Irina Dulubova, Xuelin Lou, Jun Lu, Iryna Huryeva, Amer Alam, Ralf Schneggenburger, Thomas C Südhof, Josep Rizo

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 151 papers.

0numbers the graph read from it
0cells of the map it votes in
151citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

151 citing papers in PubMed, 291 citations in OpenAlex.

  1. Article
  2. The Synaptic Vesicle Priming Protein Munc13 Mediates Evoked Somatodendritic Dopamine Release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026
    Article
  3. Article
  4. Article
  5. Munc13 serves as a molecular filter for SNARE sorting and assembly in active zone condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Disruption of a selective vesicle pool upon retrograde amnesia dissociates memory at presynaptic terminals.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. A specific negatively charged sequence confers intramolecular regulation on Munc13-1 function in synaptic exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

91 more citing papers are in PubMed but not listed here.

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

8 authors at 2 institutions in 2 countries.

Irina DulubovaDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390-8816, USA.
Xuelin Lou
Jun Lu
Iryna Huryeva
Amer Alam
Ralf Schneggenburger
Thomas C Südhof
Josep Rizo
The University of Texas Southwestern Medical Center · USMax Planck Institute for Biophysical Chemistry · DE

Funding

SYNAPTOTAGMIN AND C2 DOMAINS--STRUCTURE AND FUNCTIONR01NS040944 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI RIZOREY, JOSE · 2001 to 2016
$6.4M
NINDS NIH HHS NS40944NINDS NIH HHS R01 NS040944
6 · The paper itself

Abstract

alpha-RIMs and Munc13s are active zone proteins that control priming of synaptic vesicles to a readily releasable state, and interact with each other via their N-terminal sequences. The alpha-RIM N-terminal sequence also binds to Rab3s (small synaptic vesicle GTPases), an interaction that regulates presynaptic plasticity. We now demonstrate that alpha-RIMs contain adjacent but separate Munc13- and Rab3-binding sites, allowing formation of a tripartite Rab3/RIM/Munc13 complex. Munc13 binding is mediated by the alpha-RIM zinc-finger domain. Elucidation of the three-dimensional structure of this domain by NMR spectroscopy facilitated the design of a mutation that abolishes alpha-RIM/Munc13 binding. Selective disruption of this interaction in the calyx of Held synapse decreased the size of the readily releasable vesicle pool. Our data suggest that the ternary Rab3/RIM/Munc13 interaction approximates synaptic vesicles to the priming machinery, providing a substrate for presynaptic plasticity. The modular architecture of alpha-RIMs, with nested binding sites for Rab3 and other targets, may be a general feature of Rab effectors that share homology with the alpha-RIM N-terminal sequence.

Indexed as

Models, MolecularAmino Acid SequenceBinding SitesCalorimetryElectrophysiologyEscherichia coliGlutathione TransferaseGTP-Binding ProteinsHumansMolecular Sequence DataMultiprotein ComplexesMutagenesisNerve Tissue ProteinsNuclear Magnetic Resonance, Biomolecularrab3 GTP-Binding ProteinsSequence AlignmentGlutathione TransferaseGTP-Binding ProteinsMultiprotein ComplexesNerve Tissue Proteinsrab3 GTP-Binding ProteinsRim protein, mammalianUNC13B protein, human

Identifiers

PMID16052212
PMCPMC1187938
OpenAlexW2125278970

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.