Evidence map›Paper›PMID 19563813›Full record

ArticleJournal of molecular biology2009

Remote homology between Munc13 MUN domain and vesicle tethering complexes.

Jimin Pei, Cong Ma, Josep Rizo, Nick V Grishin

Abstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.2field-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

56 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. GARP Complex in Golgi Physiology.Sub-cellular biochemistry · 2026
    Review
  5. Article
  6. BiallelicInternational journal of molecular sciences · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Role of GARP Vesicle Tethering Complex in Golgi Physiology.International journal of molecular sciences · 2023
    Review
  11. SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023
    Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Ferlins and TgDOC2 inLife (Basel, Switzerland) · 2021
    Article
  17. Review
  18. Article
  19. Article
  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

4 authors at 3 institutions in 1 country.

Jimin PeiHoward Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. jpei@chop.swmed.edu
Cong Ma
Josep Rizo
Nick V Grishin
The University of Texas Southwestern Medical Center · USHoward Hughes Medical Institute · USSouthwestern Medical Center · US

Funding

STRUCTURE/FUNCTION OF SYNTAXIN 1R01NS037200 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI RIZOREY, JOSE · 1998 to 2016
$6.5M
Computations of Fold Changes in Evolution of ProteinsR01GM067165 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GRISHIN, NICK V. · 2003 to 2006
$1.1M
Howard Hughes Medical InstituteNIGMS NIH HHS GM67165NIGMS NIH HHS R01 GM067165NINDS NIH HHS NS37200NINDS NIH HHS R01 NS037200
6 · The paper itself

Abstract

Most core components of the neurotransmitter release machinery have homologues in other types of intracellular membrane traffic, likely underlying a universal mechanism of intracellular membrane fusion. However, no clear similarity between Munc13s and protein families generally involved in membrane traffic has been reported, despite the essential nature of Munc13s for neurotransmitter release. This crucial function was ascribed to a minimal Munc13 region called the MUN domain, which likely participates in soluble N-ethylmaleimide sensitive factor attachment protein receptor complex (SNARE) assembly and is also found in Ca(2+)-dependent activator protein for secretion. We have now used comparative sequence and structural analyses to study the structure and evolutionary origin of the MUN domain. We found weak yet significant sequence similarities between the MUN domain and a set of protein subunits from several related vesicle tethering complexes, such as Sec6 from the exocyst complex and Vps53 from the Golgi-associated retrograde protein complex. Such an evolutionary relationship allows structure prediction of the MUN domain and suggests functional similarities between MUN domain-containing proteins and multisubunit tethering complexes such as exocyst, conserved oligomeric Golgi complex, Golgi-associated retrograde protein complex, and Dsl1p. These findings further unify the mechanism of neurotransmitter release with those of other types of intracellular membrane traffic and, in turn, support a role for tethering complexes in soluble N-ethylmaleimide sensitive factor attachment protein receptor complex assembly.

Indexed as

Amino Acid SequenceAnimalsBiological TransportCalciumEvolution, MolecularGolgi ApparatusHumansIntracellular MembranesMembrane FusionMembrane ProteinsMolecular Sequence DataMultiprotein ComplexesNerve Tissue ProteinsNeurotransmitter AgentsPhylogenyProtein Structure, SecondaryCalciumMembrane ProteinsMultiprotein ComplexesNerve Tissue ProteinsNeurotransmitter AgentsProtein SubunitsVesicular Transport Proteins

Identifiers

PMID19563813
PMCPMC3158588
OpenAlexW2029981873

What OpenQuestion holds

Textmetadata
LicenceTDM
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.