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Phosphorylation of hnRNP K by cyclin-dependent kinase 2 controls cytosolic accumulation of TDP-43
Cytosolic accumulation of TAR DNA binding protein 43 (TDP-43) is a major neuropathological feature of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). However, the mechanisms involved in TDP-43 accumulation remain largely unknown. Previously, we reported that inhibitors of cyclin-dependent kinases (CDKs) prevented cytosolic stress granule accumulation of TDP-43, correlating with depletion of heterogeneous ribonucleoprotein (hnRNP) K from stress granules. In the present study, we further investigated the relationship between TDP-43 and hnRNP K and their control by CDKs. Inhibition of CDK2 ab...
Source: Human Molecular Genetics - February 19, 2015 Category: Genetics & Stem Cells Authors: Moujalled, D., James, J. L., Yang, S., Zhang, K., Duncan, C., Moujalled, D. M., Parker, S. J., Caragounis, A., Lidgerwood, G., Turner, B. J., Atkin, J. D., Grubman, A., Liddell, J. R., Proepper, C., Boeckers, T. M., Kanninen, K. M., Blair, I., Crouch, P. Tags: ARTICLES Source Type: research

TARDBP pathogenic mutations increase cytoplasmic translocation of TDP-43 and cause reduction of endoplasmic reticulum Ca(2+) signaling in motor neurons.
Abstract The transactive response DNA binding protein (TDP-43) is a major component of the characteristic neuronal cytoplasmic inclusions seen in amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Furthermore, pathogenic mutations in the gene encoding TDP-43, TARDBP, are found in sporadic and familial ALS cases. To study the molecular mechanisms of cellular toxicity due to TDP-43 mutations we generated a novel in vitro cellular model using a fluorescently tagged human genomic TARDBP locus carrying one of two ALS-associated mutations, A382T or M337V, which were used to generate site-specific bac...
Source: Neurobiology of Disease - December 17, 2014 Category: Neurology Authors: Mutihac R, Alegre-Abarrategui J, Gordon D, Farrimond L, Yamasaki-Mann M, Talbot K, Wade-Martins R Tags: Neurobiol Dis Source Type: research

δ‐Opioid Receptors Up‐regulate Excitatory Amino Acid Transporters in Mouse Astrocytes
Conclusions and ImplicationsDOR activation upregulates astrocytic EAATs via MEK‐ERK‐p38 signaling, suggesting a critical role of DOR in the regulation of astrocytic EAATs and neuroprotection against excitotoxic injury. Since decreased EAAT expression contributes to pathophysiology in many neurological diseases such as amyotrophic lateral sclerosis, our findings present a new platform for potential treatments of these diseases.
Source: British Journal of Pharmacology - July 23, 2014 Category: Drugs & Pharmacology Authors: Jianfeng Liang, Dongman Chao, Harleen K Sandhu, Yanbing Yu, Li Zhang, Gianfranco Balboni, Dong H Kim, Ying Xia Tags: Research Paper Source Type: research

VAPB/ALS8 interacts with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase
Conclusions: The FFAT-like motifs we identified in FAF1 and ASNA1 demonstrate that sequences containing a single phenylalanine residue with the consensus (D/E)(D/E)FEDAx(D/E) are also proficient to mediate interaction with VAPB.Our findings indicate that the repertoire of VAPB interactors is more diverse than previously anticipated and link VAPB to the function of ATPase complexes such as p97/FAF1 and ASNA1/TRC.
Source: BMC Biology - Latest articles - May 29, 2014 Category: Biology Authors: Yorann BaronPatrick PedrioliKshitiz TyagiClare JohnsonNicola WoodDaniel FountaineMelanie WightmanGabriela Alexandru Source Type: research

Functional Interaction between Amyloid-β Precursor Protein and Peripherin Neurofilaments: A Shared Pathway Leading to Alzheimer's Disease and Amyotrophic Lateral Sclerosis?
Conclusion: Our results indicate that a fraction of APP is cleaved by β-secretase in the soma and that the generated sAPP becomes associated with perinuclear peripherin neurofilaments. These findings link the metabolism of APP - which is dysregulated in AD - to the organization of neurofilaments - which is abnormal in ALS - and suggest a possible crosstalk/overlap between the molecular mechanisms of these diseases. PMID: 24009040 [PubMed - as supplied by publisher]
Source: Neuro-Degenerative Diseases - September 4, 2013 Category: Neurology Authors: Muresan V, Villegas C, Ladescu Muresan Z Tags: Neurodegener Dis Source Type: research

Optineurin suppression causes neuronal cell death via NF‐κB pathway
This article is protected by copyright. All rights reserved.
Source: Journal of Neurochemistry - June 1, 2013 Category: Neurology Authors: Mayumi Akizuki, Hirofumi Yamashita, Kengo Uemura, Hirofumi Maruyama, Hideshi Kawakami, Hidefumi Ito, Ryosuke Takahashi Tags: Short Communication Source Type: research

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