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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Myosin Va interacts with the exosomal protein spermine synthase

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Author(s):
Dolce, Luciano G. [1, 2] ; Silva-Junior, Rui M. P. [3] ; Assis, Leandro H. P. [1, 2] ; Nascimento, Andrey F. Z. [4, 2] ; Araujo, Jackeline S. [3] ; Meschede, Ingrid P. [3] ; Espreafico, Enilza M. [3] ; de Giuseppe, Priscila O. [5, 1] ; Murakami, Mario T. [5, 1]
Total Authors: 9
Affiliation:
[1] Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Biosci Natl Lab LNBio, BR-13083970 Campinas, SP - Brazil
[2] Univ Estadual Campinas, Inst Biol, Grad Program Funct & Mol Biol, Campinas, SP - Brazil
[3] Univ Sao Paulo, Fac Med Ribeirao Preto, Dept Cell & Mol Biol, Ribeirao Preto, SP - Brazil
[4] Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Synchrotron Light Lab LNLS, BR-13083970 Campinas, SP - Brazil
[5] Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Bioethanol Sci & Technol Lab CTBE, BR-13083970 Campinas, SP - Brazil
Total Affiliations: 5
Document type: Journal article
Source: BIOSCIENCE REPORTS; v. 39, n. 3 MAR 29 2019.
Web of Science Citations: 1
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 SMSwas further validated in vitro and displayed a Kd in the low micromolar range (3.5+-0.5 mu M). 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. (AU)

FAPESP's process: 14/09720-9 - Studies of the role of phosphorylation and protein binding partners in regulating the function of human class V myosins
Grantee:Mário Tyago Murakami
Support type: Regular Research Grants
FAPESP's process: 11/20229-7 - Human myosin-5A and the intracellular transport of cargoes: studies of the myosin-5A and adapter proteins complexes
Grantee:Leandro Henrique de Paula Assis
Support type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 14/00584-5 - Understanding the role of phosphorylation cargo binding domain (CBD) in the regulation of unconventional myosins Class V
Grantee:Luciano Graciani Dolce
Support type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 14/03989-6 - Uncovering pathophysiological and molecular mechanisms involved in tumorigenesis by platforms for next-generation sequencing (NGS)
Grantee:Margaret de Castro
Support type: Research Projects - Thematic Grants
FAPESP's process: 09/14257-8 - Structural studies of the globular domain of human myosin Va responsible for intracellular transport of organelles and vesicles
Grantee:Andrey Fabricio Ziem Nascimento
Support type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 16/10862-8 - Study of myosin-Va role in the processes of mitochondrial dynamics and mitophagy
Grantee:Jackeline Souza Araújo
Support type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 18/04017-9 - Genomic and functional characterization of putative melanoma-restricted lncRNAs (RMELs)
Grantee:Enilza Maria Espreafico
Support type: Regular Research Grants
FAPESP's process: 13/08135-2 - CTC - Center for Cell-Based Therapy
Grantee:Dimas Tadeu Covas
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC