Loss of ISWI Function in Drosophila Nuclear Bodies Drives Cytoplasmic Redistribution of Drosophila TDP-43
| Autor: | Luca Lo Piccolo, Davide Corona, Giorgio Giurato, Maria Cristina Onorati, Martina Sollazzo, Rosa Bonaccorso, Antonia M. R. Ingrassia, Fabian Feiguin, Lorenzo Li Greci, Giulia Romano, Andrea Attardi |
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| Přispěvatelé: | Lo Piccolo L., Bonaccorso R., Attardi A., Li Greci L., Romano G., Sollazzo M., Giurato G., Ingrassia A.M.R., Feiguin F., Corona D.F.V., Onorati M.C. |
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Cytoplasm Cytoplasmic inclusion Fluorescent Antibody Technique Protein aggregation Heterogeneous ribonucleoprotein particle Heterogeneous-Nuclear Ribonucleoproteins lcsh:Chemistry 0302 clinical medicine Drosophila Proteins neurodegenerative diseases nuclear body lcsh:QH301-705.5 Spectroscopy General Medicine hnRNPs Computer Science Applications Cell biology Chromatin Transport protein DNA-Binding Proteins Protein Transport medicine.anatomical_structure Drosophila Drosophila Protein Protein Binding Imitation SWI Biology Catalysis Article Inorganic Chemistry omega speckles 03 medical and health sciences medicine Animals Physical and Theoretical Chemistry Molecular Biology Genetic Association Studies Cell Nucleus Organic Chemistry ta1182 Chromatin Assembly and Disassembly Cell nucleus 030104 developmental biology lcsh:Biology (General) lcsh:QD1-999 gene expression dTDP-43 gene regulation 030217 neurology & neurosurgery |
| Zdroj: | International Journal of Molecular Sciences International Journal of Molecular Sciences; Volume 19; Issue 4; Pages: 1082 International Journal of Molecular Sciences, Vol 19, Iss 4, p 1082 (2018) |
| ISSN: | 1422-0067 |
| Popis: | Over the past decade, evidence has identified a link between protein aggregation, RNA biology, and a subset of degenerative diseases. An important feature of these disorders is the cytoplasmic or nuclear aggregation of RNA-binding proteins (RBPs). Redistribution of RBPs, such as the human TAR DNA-binding 43 protein (TDP-43) from the nucleus to cytoplasmic inclusions is a pathological feature of several diseases. Indeed, sporadic and familial forms of amyotrophic lateral sclerosis (ALS) and fronto-temporal lobar degeneration share as hallmarks ubiquitin-positive inclusions. Recently, the wide spectrum of neurodegenerative diseases characterized by RBPs functions’ alteration and loss was collectively named proteinopathies. Here, we show that TBPH (TAR DNA-binding protein-43 homolog), the Drosophila ortholog of human TDP-43 TAR DNA-binding protein-43, interacts with the arcRNA hsrω and with hsrω-associated hnRNPs. Additionally, we found that the loss of the omega speckles remodeler ISWI (Imitation SWI) changes the TBPH sub-cellular localization to drive a TBPH cytoplasmic accumulation. Our results, hence, identify TBPH as a new component of omega speckles and highlight a role of chromatin remodelers in hnRNPs nuclear compartmentalization. |
| Databáze: | OpenAIRE |
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