Myosin Va interacts with the exosomal protein spermine synthase
| Autor: | A.F.Z. Nascimento, Rui M.P. da Silva-Júnior, Leandro H.P. Assis, Jackeline S. Araujo, Mário T. Murakami, Priscila Oliveira de Giuseppe, Enilza Maria Espreáfico, Luciano G. Dolce, I. P. Meschede |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Spermidine protein-protein interactions exosome transport Exosomes Biochemistry myosins 0302 clinical medicine Myosin Griscelli syndrome Research Articles Cellular localization Cells Cultured biology Chemistry cytoskeleton Cell biology Protein Transport Spermine synthase MCF-7 Cells RNA Interference polyamine synthesis exocytosis transcription Research Article Protein Binding Snyder Robinson mental retardation syndrome cellular localization Myosin Type V Spermine Synthase Biophysics Exocytosis Protein–protein interaction 03 medical and health sciences trafficking Cell Line Tumor Two-Hybrid System Techniques Commentaries Molecular motor Animals Humans Molecular Biology Actin Binding Sites Myosin Heavy Chains myosin superfamily Cytoplasmic Vesicles EXPRESSÃO GÊNICA Cell Biology Fibroblasts Microvesicles 030104 developmental biology Gene Expression Regulation Mental Retardation X-Linked biology.protein Commentary Spermine 030217 neurology & neurosurgery |
| Zdroj: | Bioscience Reports Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP |
| ISSN: | 1573-4935 |
| Popis: | A recent paper in Bioscience Reports (BSR20182189) describes the discovery of an interaction between the motor protein myosin Va and the metabolic enzyme spermine synthase. Myosin Va is a molecular motor which plays a key role in vesicle transport. Mutations in the gene which encodes this protein are associated with Griscelli syndrome type 1 and the ‘dilute’ phenotype in animals. Spermine synthase catalyzes the conversion of spermidine to spermine. This largely cytoplasmic enzyme can also be localized to the soluble fraction in exosomes. Mutations in the spermine synthase gene are associated with Snyder Robinson mental retardation syndrome. The interaction between the two proteins was detected using the yeast two hybrid method and verified by microscale thermophoresis of recombinant proteins. Knockdown of the MYO5A gene reduced the expression of mRNA coding for spermine synthase. The amount of this transcript was also reduced in cells derived from a patient with Griscelli syndrome type 1. This suggests that, in addition to a direct physical interaction between the two proteins, myosin Va also modulates the transcription of the spermine synthase gene. The mechanism for this modulation is currently unknown. These findings have implications for Griscelli syndrome type 1 and Snyder Robinson mental retardation syndrome. They also suggest that interactions between myosin Va and soluble exosome proteins such as spermine synthase may be important in the mechanism of exosome transport. |
| Databáze: | OpenAIRE |
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