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Myosin Va interacts with the exosomal protein spermine synthase

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 sti...

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Autores principales: 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.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6395372/
https://www.ncbi.nlm.nih.gov/pubmed/30733278
http://dx.doi.org/10.1042/BSR20182189
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author 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.
author_facet 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.
author_sort Dolce, Luciano G.
collection PubMed
description 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 K(d) 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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spelling pubmed-63953722019-03-07 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. Biosci Rep Research Articles 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 K(d) 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. Portland Press Ltd. 2019-03-01 /pmc/articles/PMC6395372/ /pubmed/30733278 http://dx.doi.org/10.1042/BSR20182189 Text en © 2019 The Author(s). http://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (http://creativecommons.org/licenses/by/4.0/) .
spellingShingle Research Articles
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.
Myosin Va interacts with the exosomal protein spermine synthase
title Myosin Va interacts with the exosomal protein spermine synthase
title_full Myosin Va interacts with the exosomal protein spermine synthase
title_fullStr Myosin Va interacts with the exosomal protein spermine synthase
title_full_unstemmed Myosin Va interacts with the exosomal protein spermine synthase
title_short Myosin Va interacts with the exosomal protein spermine synthase
title_sort myosin va interacts with the exosomal protein spermine synthase
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6395372/
https://www.ncbi.nlm.nih.gov/pubmed/30733278
http://dx.doi.org/10.1042/BSR20182189
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