A1 Refereed original research article in a scientific journal
Loss of ISWI Function in Drosophila Nuclear Bodies Drives Cytoplasmic Redistribution of Drosophila TDP-43
Authors: Lo Piccolo L, Bonaccorso R, Attardi A, Li Greci L, Romano G, Sollazzo M, Giurato G, Ingrassia AMR, Feiguin F, Corona DFV, Onorati MC
Publisher: MDPI
Publication year: 2018
Journal:International Journal of Molecular Sciences
Journal name in sourceINTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Journal acronym: INT J MOL SCI
Article number: ARTN 1082
Volume: 19
Issue: 4
Number of pages: 15
ISSN: 1422-0067
DOI: https://doi.org/10.3390/ijms19041082
Self-archived copy’s web address: https://research.utu.fi/converis/portal/detail/Publication/32521124
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 hsr omega and with hsr omega-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.
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