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Myosin Va interacts with the exosomal protein spermine synthase.
Dolce, Luciano G; Silva-Junior, Rui M P; Assis, Leandro H P; Nascimento, Andrey F Z; Araujo, Jackeline S; Meschede, Ingrid P; Espreafico, Enilza M; de Giuseppe, Priscila O; Murakami, Mário T.
Afiliación
  • Dolce LG; Graduate Program in Functional and Molecular Biology, Institute of Biology, University of Campinas, Campinas, São Paulo, Brazil.
  • Silva-Junior RMP; Brazilian Biosciences National Laboratory (LNBio), Brazilian Center for Research in Energy and Materials (CNPEM), Zip Code 13083-970, Campinas, São Paulo, Brazil.
  • Assis LHP; Department of Cell and Molecular Biology, Faculty of Medicine of Ribeirão Preto, University of São Paulo, Ribeirão Preto, São Paulo, Brazil.
  • Nascimento AFZ; Graduate Program in Functional and Molecular Biology, Institute of Biology, University of Campinas, Campinas, São Paulo, Brazil.
  • Araujo JS; Brazilian Biosciences National Laboratory (LNBio), Brazilian Center for Research in Energy and Materials (CNPEM), Zip Code 13083-970, Campinas, São Paulo, Brazil.
  • Meschede IP; Graduate Program in Functional and Molecular Biology, Institute of Biology, University of Campinas, Campinas, São Paulo, Brazil.
  • Espreafico EM; Brazilian Synchrotron Light Laboratory (LNLS), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, Zip code 13083-970, São Paulo, Brazil.
  • de Giuseppe PO; Department of Cell and Molecular Biology, Faculty of Medicine of Ribeirão Preto, University of São Paulo, Ribeirão Preto, São Paulo, Brazil.
  • Murakami MT; Department of Cell and Molecular Biology, Faculty of Medicine of Ribeirão Preto, University of São Paulo, Ribeirão Preto, São Paulo, Brazil.
Biosci Rep ; 39(3)2019 03 29.
Article en En | MEDLINE | ID: mdl-30733278
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 in vitro and displayed a Kd in the low micromolar range (3.5 ± 0.5 µM). SMS localized together with MyoVa in cytoplasmic vesicles of breast cancer MCF-7 and neuroblastoma SH-SY5Y cell lines, known to produce exosomes. Moreover, MYO5A knockdown decreased the expression of SMS gene and rendered the distribution of SMS protein diffuse, supporting a role for MyoVa in SMS expression and targeting.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Espermina Sintasa / Cadenas Pesadas de Miosina / Vesículas Citoplasmáticas / Miosina Tipo V / Exosomas Límite: Humans Idioma: En Revista: Biosci Rep Año: 2019 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Espermina Sintasa / Cadenas Pesadas de Miosina / Vesículas Citoplasmáticas / Miosina Tipo V / Exosomas Límite: Humans Idioma: En Revista: Biosci Rep Año: 2019 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Reino Unido