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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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2019
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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. |
format | Online Article Text |
id | pubmed-6395372 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
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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