Evidence map›Paper›PMID 16030255›Full record

ArticleMolecular biology of the cell2005

Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A.

Michitoshi Watanabe, Kazushige Nomura, Akihiro Ohyama, Ryoki Ishikawa, Yoshiaki Komiya, Kohei Hosaka, Emiko Yamauchi, Hisaaki Taniguchi, Nobuyuki Sasakawa, Konosuke Kumakura and 4 more

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In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

36 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
  2. Article
  3. The Role of Calmodulin vs. Synaptotagmin in Exocytosis.Frontiers in molecular neuroscience · 2021
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Multiple roles for the actin cytoskeleton during regulated exocytosis.Cellular and molecular life sciences : CMLS · 2013
    Review
  16. Article
  17. Article
  18. Walking to work: roles for class V myosins as cargo transporters.Nature reviews. Molecular cell biology · 2011
    Review
  19. Article
  20. Insight into the role of Ca2+-binding protein 5 in vesicle exocytosis.Investigative ophthalmology & visual science · 2011
    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

14 authors at 5 institutions in 2 countries.

Michitoshi WatanabeDivision of Molecular and Cellular Biology, Graduate School of Medical and Dental Sciences, Niigata University, Niigata, Niigata 951-8510, Japan.
Kazushige Nomura
Akihiro Ohyama
Ryoki Ishikawa
Yoshiaki Komiya
Kohei Hosaka
Emiko Yamauchi
Hisaaki Taniguchi
Nobuyuki Sasakawa
Konosuke Kumakura
Tatsuo Ushiki
Osamu Sato
Mitsuo Ikebe
Michihiro Igarashi
Gunma University · JPNiigata University · JPLife Science Institute · JPTokushima University · JPUniversity of Massachusetts Chan Medical School · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myosin-Va is an actin-based processive motor that conveys intracellular cargoes. Synaptic vesicles are one of the most important cargoes for myosin-Va, but the role of mammalian myosin-Va in secretion is less clear than for its yeast homologue, Myo2p. In the current studies, we show that myosin-Va on synaptic vesicles interacts with syntaxin-1A, a t-SNARE involved in exocytosis, at or above 0.3 microM Ca2+. Interference with formation of the syntaxin-1A-myosin-Va complex reduces the exocytotic frequency in chromaffin cells. Surprisingly, the syntaxin-1A-binding site was not in the tail of myosin-Va but rather in the neck, a region that contains calmodulin-binding IQ-motifs. Furthermore, we found that syntaxin-1A binding by myosin-Va in the presence of Ca2+ depends on the release of calmodulin from the myosin-Va neck, allowing syntaxin-1A to occupy the vacant IQ-motif. Using an anti-myosin-Va neck antibody, which blocks this binding, we demonstrated that the step most important for the antibody's inhibitory activity is the late sustained phase, which is involved in supplying readily releasable vesicles. Our results demonstrate that the interaction between myosin-Va and syntaxin-1A is involved in exocytosis and suggest that the myosin-Va neck contributes not only to the large step size but also to the regulation of exocytosis by Ca2+.

Indexed as

Amino Acid SequenceAnimalsBrainCalciumCells, CulturedChromaffin CellsExocytosisMicroscopy, Atomic ForceMolecular Sequence DataMyosin Heavy ChainsMyosin Type VProtein BindingRatsSynaptic VesiclesSyntaxin 1CalciumMyo5a protein, ratMyosin Heavy ChainsMyosin Type VSyntaxin 1

Identifiers

PMID16030255
PMCPMC1237061
OpenAlexW2141610168

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.