Protein Disulfide Isomerase Endoplasmic Reticulum Protein 57 (ERp57) is Protective Against ALS-Associated Mutant TDP-43 in Neuronal Cells

Acewicz, A., Stępień, T., Felczak, P., Tarka, S., & Wierzba-Bobrowicz, T. (2022). Incidence and morphology of secondary TDP-43 proteinopathies: Part 1. Folia Neuropathologica, 60(3), 267–276. https://doi.org/10.5114/fn.2022.120314

Article  PubMed  Google Scholar 

Bargsted, L., Hetz, C., & Matus, S. (2016). ERp57 in neurodegeneration and regeneration. Neural Regeneration Research, 11(2), 232–233. https://doi.org/10.4103/1673-5374.177722

Article  CAS  PubMed  PubMed Central  Google Scholar 

Barmada, S. J., Serio, A., Arjun, A., Bilican, B., Daub, A., Ando, D. M., Tsvetkov, A., Pleiss, M., Li, X., Peisach, D., Shaw, C., Chandran, S., & Finkbeiner, S. (2014). Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models. Nature Chemical Biology, 10(8), 677–685. https://doi.org/10.1038/nchembio.1563

Article  CAS  PubMed  PubMed Central  Google Scholar 

Barmada, S. J., Skibinski, G., Korb, E., Rao, E. J., Wu, J. Y., & Finkbeiner, S. (2010). Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis. Journal of Neuroscience, 30(2), 639–649. https://doi.org/10.1523/jneurosci.4988-09.2010

Article  CAS  PubMed  Google Scholar 

Bilches Medinas, D., Malik, S., Yildiz-Bölükbasi, E., Borgonovo, J., Saaranen, M. J., Urra, H., Pulgar, E., Afzal, M., Contreras, D., Wright, M. T., Bodaleo, F., Quiroz, G., Rozas, P., Mumtaz, S., Díaz, R., Rozas, C., Cabral-Miranda, F., Piña, R., Valenzuela, V., … Tolun, A. (2022). Mutation in protein disulfide isomerase A3 causes neurodevelopmental defects by disturbing endoplasmic reticulum proteostasis. EMBO Journal, 41(2), e105531. https://doi.org/10.15252/embj.2020105531

Article  CAS  PubMed  Google Scholar 

Chen, M. Z., Moily, N. S., Bridgford, J. L., Wood, R. J., Radwan, M., Smith, T. A., Song, Z., Tang, B. Z., Tilley, L., Xu, X., Reid, G. E., Pouladi, M. A., Hong, Y., & Hatters, D. M. (2017). A thiol probe for measuring unfolded protein load and proteostasis in cells. Nature Communications, 8(1), 474. https://doi.org/10.1038/s41467-017-00203-5

Article  CAS  PubMed  PubMed Central  Google Scholar 

Chen, X., Shi, C., He, M., Xiong, S., & Xia, X. (2023). Endoplasmic reticulum stress: Molecular mechanism and therapeutic targets. Signal Transduction and Targeted Therapy, 8(1), 352. https://doi.org/10.1038/s41392-023-01570-w

Article  CAS  PubMed  PubMed Central  Google Scholar 

Chichiarelli, S., Altieri, F., Paglia, G., Rubini, E., Minacori, M., & Eufemi, M. (2022). ERp57/PDIA3: New insight. Cellular & Molecular Biology Letters, 27(1), 12. https://doi.org/10.1186/s11658-022-00315-x

Article  CAS  Google Scholar 

Cohen, T. J., Hwang, A. W., Unger, T., Trojanowski, J. Q., & Lee, V. M. (2012). Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking. EMBO Journal, 31(5), 1241–1252. https://doi.org/10.1038/emboj.2011.471

Article  CAS  PubMed  Google Scholar 

Corcia, P., Valdmanis, P., Millecamps, S., Lionnet, C., Blasco, H., Mouzat, K., Daoud, H., Belzil, V., Morales, R., Pageot, N., Danel-Brunaud, V., Vandenberghe, N., Pradat, P. F., Couratier, P., Salachas, F., Lumbroso, S., Rouleau, G. A., Meininger, V., & Camu, W. (2012). Phenotype and genotype analysis in amyotrophic lateral sclerosis with TARDBP gene mutations. Neurology, 78(19), 1519–1526. https://doi.org/10.1212/WNL.0b013e3182553c88

Article  CAS  PubMed  Google Scholar 

Dmitrieva, N. I., & Burg, M. B. (2008). Analysis of DNA breaks, DNA damage response, and apoptosis produced by high NaCl. American Journal of Physiology. Renal Physiology, 295(6), F1678–F1688. https://doi.org/10.1152/ajprenal.90424.2008

Article  CAS  PubMed  PubMed Central  Google Scholar 

Farrawell, N. E., Lambert-Smith, I. A., Warraich, S. T., Blair, I. P., Saunders, D. N., Hatters, D. M., & Yerbury, J. J. (2015). Distinct partitioning of ALS associated TDP-43, FUS and SOD1 mutants into cellular inclusions. Science and Reports, 5, 13416. https://doi.org/10.1038/srep13416

Article  CAS  Google Scholar 

Frickel, E. M., Frei, P., Bouvier, M., Stafford, W. F., Helenius, A., Glockshuber, R., & Ellgaard, L. (2004). ERp57 is a multifunctional thiol-disulfide oxidoreductase. Journal of Biological Chemistry, 279(18), 18277–18287. https://doi.org/10.1074/jbc.M314089200

Article  CAS  PubMed  Google Scholar 

Gonzalez-Perez, P., Woehlbier, U., Chian, R. J., Sapp, P., Rouleau, G. A., Leblond, C. S., Daoud, H., Dion, P. A., Landers, J. E., Hetz, C., & Brown, R. H. (2015). Identification of rare protein disulfide isomerase gene variants in amyotrophic lateral sclerosis patients. Gene, 566(2), 158–165. https://doi.org/10.1016/j.gene.2015.04.035

Article  CAS  PubMed  PubMed Central  Google Scholar 

Jeon, G. S., Nakamura, T., Lee, J. S., Choi, W. J., Ahn, S. W., Lee, K. W., Sung, J. J., & Lipton, S. A. (2014). Potential effect of S-nitrosylated protein disulfide isomerase on mutant SOD1 aggregation and neuronal cell death in amyotrophic lateral sclerosis. Molecular Neurobiology, 49(2), 796–807. https://doi.org/10.1007/s12035-013-8562-z

Article  CAS  PubMed  Google Scholar 

Jessop, C. E., Chakravarthi, S., Garbi, N., Hämmerling, G. J., Lovell, S., & Bulleid, N. J. (2007). ERp57 is essential for efficient folding of glycoproteins sharing common structural domains. The EMBO Journal, 26(1), 28–40.

Article  CAS  PubMed  Google Scholar 

Jessop, C. E., Watkins, R. H., Simmons, J. J., Tasab, M., & Bulleid, N. J. (2009). Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins. Journal of Cell Science, 122(Pt 23), 4287–4295. https://doi.org/10.1242/jcs.059154

Article  CAS  PubMed  PubMed Central  Google Scholar 

Jiang, L. L., Xue, W., Hong, J. Y., Zhang, J. T., Li, M. J., Yu, S. N., He, J. H., & Hu, H. Y. (2017). The N-terminal dimerization is required for TDP-43 splicing activity. Science and Reports, 7(1), 6196. https://doi.org/10.1038/s41598-017-06263-3

Article  CAS  Google Scholar 

Jo, M., Lee, S., Jeon, Y.-M., Kim, S., Kwon, Y., & Kim, H.-J. (2020). The role of TDP-43 propagation in neurodegenerative diseases: Integrating insights from clinical and experimental studies. Experimental & Molecular Medicine, 52(10), 1652–1662. https://doi.org/10.1038/s12276-020-00513-7

Article  CAS  Google Scholar 

Klim, J. R., Pintacuda, G., Nash, L. A., Juan, I. G. S., & Eggan, K. (2021). Connecting TDP-43 pathology with neuropathy. Trends in Neurosciences, 44(6), 424–440. https://doi.org/10.1016/j.tins.2021.02.008

Article  CAS  PubMed  Google Scholar 

Maattanen, P., Kozlov, G., Gehring, K., & Thomas, D. Y. (2006). ERp57 and PDI: Multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations. Biochemistry and Cell Biology, 84(6), 881–889. https://doi.org/10.1139/o06-186

Article  CAS  PubMed  Google Scholar 

Mackenzie, I. R., Bigio, E. H., Ince, P. G., Geser, F., Neumann, M., Cairns, N. J., Kwong, L. K., Forman, M. S., Ravits, J., Stewart, H., Eisen, A., McClusky, L., Kretzschmar, H. A., Monoranu, C. M., Highley, J. R., Kirby, J., Siddique, T., Shaw, P. J., Lee, V.M.-Y., & Trojanowski, J. Q. (2007). Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations. Annals of Neurology, 61(5), 427–434. https://doi.org/10.1002/ana.21147

Article  CAS  PubMed  Google Scholar 

Maekawa, S., Leigh, P. N., King, A., Jones, E., Steele, J. C., Bodi, I., Shaw, C. E., Hortobagyi, T., & Al-Sarraj, S. (2009). TDP-43 is consistently co-localized with ubiquitinated inclusions in sporadic and guam amyotrophic lateral sclerosis but not in familial amyotrophic lateral sclerosis with and without SOD1 mutations. Neuropathology, 29(6), 672–683. https://doi.org/10.1111/j.1440-1789.2009.01029.x

Article  PubMed  Google Scholar 

Mandelkow, R., Gümbel, D., Ahrend, H., Kaul, A., Zimmermann, U., Burchardt, M., & Stope, M. B. (2017). Detection and quantification of nuclear morphology changes in apoptotic cells by fluorescence microscopy and subsequent analysis of visualized fluorescent signals. Anticancer Research, 37(5), 2239–2244. https://doi.org/10.21873/anticanres.11560

Article  CAS  PubMed  Google Scholar 

Mead, R. J., Shan, N., Reiser, H. J., Marshall, F., & Shaw, P. J. (2023). Amyotrophic lateral sclerosis: A neurodegenerative disorder poised for successful therapeutic translation. Nature Reviews Drug Discovery, 22(3), 185–212.

Article  CAS  PubMed  Google Scholar 

Meneses, A., Koga, S., O’Leary, J., Dickson, D. W., Bu, G., & Zhao, N. (2021). TDP-43 Pathology in Alzheimer’s Disease. Molecular Neurodegeneration,

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