C-Jun N-terminal kinase controls TDP-43 accumulation in stress granules induced by oxidative stress View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2011-12

AUTHORS

Jodi Meyerowitz, Sarah J Parker, Laura J Vella, Dominic CH Ng, Katherine A Price, Jeffrey R Liddell, Aphrodite Caragounis, Qiao-Xin Li, Colin L Masters, Takashi Nonaka, Masato Hasegawa, Marie A Bogoyevitch, Katja M Kanninen, Peter J Crouch, Anthony R White

ABSTRACT

BACKGROUND: TDP-43 proteinopathies are characterized by loss of nuclear TDP-43 expression and formation of C-terminal TDP-43 fragmentation and accumulation in the cytoplasm. Recent studies have shown that TDP-43 can accumulate in RNA stress granules (SGs) in response to cell stresses and this could be associated with subsequent formation of TDP-43 ubiquinated protein aggregates. However, the initial mechanisms controlling endogenous TDP-43 accumulation in SGs during chronic disease are not understood. In this study we investigated the mechanism of TDP-43 processing and accumulation in SGs in SH-SY5Y neuronal-like cells exposed to chronic oxidative stress. Cell cultures were treated overnight with the mitochondrial inhibitor paraquat and examined for TDP-43 and SG processing. RESULTS: We found that mild stress induced by paraquat led to formation of TDP-43 and HuR-positive SGs, a proportion of which were ubiquitinated. The co-localization of TDP-43 with SGs could be fully prevented by inhibition of c-Jun N-terminal kinase (JNK). JNK inhibition did not prevent formation of HuR-positive SGs and did not prevent diffuse TDP-43 accumulation in the cytosol. In contrast, ERK or p38 inhibition prevented formation of both TDP-43 and HuR-positive SGs. JNK inhibition also inhibited TDP-43 SG localization in cells acutely treated with sodium arsenite and reduced the number of aggregates per cell in cultures transfected with C-terminal TDP-43 162-414 and 219-414 constructs. CONCLUSIONS: Our studies are the first to demonstrate a critical role for kinase control of TDP-43 accumulation in SGs and may have important implications for development of treatments for FTD and ALS, targeting cell signal pathway control of TDP-43 aggregation. More... »

PAGES

57

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1186/1750-1326-6-57

DOI

http://dx.doi.org/10.1186/1750-1326-6-57

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1040323624

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/21819629


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