Evidence map›Paper›PMID 30733278›Full record

ArticleBioscience reports2019

Myosin Va interacts with the exosomal protein spermine synthase.

Luciano G Dolce, Rui M P Silva-Junior, Leandro H P Assis, Andrey F Z Nascimento, Jackeline S Araujo, Ingrid P Meschede, Enilza M Espreafico, Priscila O de Giuseppe, Mário T Murakami

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 49% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Luciano G DolceGraduate Program in Functional and Molecular Biology, Institute of Biology, University of Campinas, Campinas, São Paulo, Brazil.
Rui M P Silva-JuniorDepartment of Cell and Molecular Biology, Faculty of Medicine of Ribeirão Preto, University of São Paulo, Ribeirão Preto, São Paulo, Brazil.
Leandro H P AssisGraduate Program in Functional and Molecular Biology, Institute of Biology, University of Campinas, Campinas, São Paulo, Brazil.
Andrey F Z NascimentoGraduate Program in Functional and Molecular Biology, Institute of Biology, University of Campinas, Campinas, São Paulo, Brazil.
Jackeline S AraujoDepartment of Cell and Molecular Biology, Faculty of Medicine of Ribeirão Preto, University of São Paulo, Ribeirão Preto, São Paulo, Brazil.
Ingrid P MeschedeDepartment of Cell and Molecular Biology, Faculty of Medicine of Ribeirão Preto, University of São Paulo, Ribeirão Preto, São Paulo, Brazil.
Enilza M EspreaficoDepartment of Cell and Molecular Biology, Faculty of Medicine of Ribeirão Preto, University of São Paulo, Ribeirão Preto, São Paulo, Brazil mario.murakami@ctbe.cnpem.br priscila.giuseppe@ctbe.cnpem.br emespre@fmrp.usp.br.
Priscila O de GiuseppeBrazilian Biosciences National Laboratory (LNBio), Brazilian Center for Research in Energy and Materials (CNPEM), Zip Code 13083-970, Campinas, São Paulo, Brazil mario.murakami@ctbe.cnpem.br priscila.giuseppe@ctbe.cnpem.br emespre@fmrp.usp.br.
Mário T MurakamiBrazilian Biosciences National Laboratory (LNBio), Brazilian Center for Research in Energy and Materials (CNPEM), Zip Code 13083-970, Campinas, São Paulo, Brazil mario.murakami@ctbe.cnpem.br priscila.giuseppe@ctbe.cnpem.br emespre@fmrp.usp.br.ORCID 0000-0002-0405-8010
Universidade de São Paulo · BRUniversidade Estadual de Campinas (UNICAMP) · BRBrazilian Center for Research in Energy and Materials · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myosin Va (MyoVa) is an actin-based molecular motor that plays key roles in the final stages of secretory pathways, including neurotransmitter release. Several studies have addressed how MyoVa coordinates the trafficking of secretory vesicles, but why this molecular motor is found in exosomes is still unclear. In this work, using a yeast two-hybrid screening system, we identified the direct interaction between the globular tail domain (GTD) of MyoVa and four protein components of exosomes: the WD repeat-containing protein 48 (WDR48), the cold shock domain-containing protein E1 (CSDE1), the tandem C2 domain-containing protein 1 (TC2N), and the enzyme spermine synthase (SMS). The interaction between the GTD of MyoVa and SMS was further validated

Indexed as

Binding SitesCell Line, TumorCells, CulturedCytoplasmic VesiclesExosomesFibroblastsGene Expression RegulationHumansMCF-7 CellsMyosin Heavy ChainsMyosin Type VProtein BindingProtein TransportRNA InterferenceSpermine SynthaseTwo-Hybrid System TechniquesMYO5A protein, humanMyosin Heavy ChainsMyosin Type VSpermine Synthasecellular localizationexocytosismyosinsprotein-protein interactionstraffickingtranscription

Identifiers

PMID30733278
PMCPMC6395372
OpenAlexW2914491411

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.