Afroz T, Chevalier E, Audrain M, Dumayne C, Ziehm T, Moser R, Egesipe A-L, Mottier L, Ratnam M, Neumann M, Havas D, Ollier R, Piorkowska K, Chauhan M, Silva AB, Thapa S, Stöhr J, Bavdek A, Eligert V, Adolfsson O, Nelson PT, Porta S, Lee VM-Y, Pfeifer A, Kosco-Vilbois M, Seredenina T (2023) Immunotherapy targeting the C-terminal domain of TDP-43 decreases neuropathology and confers neuroprotection in mouse models of ALS/FTD. Neurobiol Dis 179:106050. https://doi.org/10.1016/j.nbd.2023.106050

Article  CAS  PubMed  Google Scholar 

Alfieri JA, Pino NS, Igaz LM (2014) Reversible behavioral phenotypes in a conditional mouse model of TDP-43 proteinopathies. J Neurosci 34:15244–15259. https://doi.org/10.1523/JNEUROSCI.1918-14.2014

Article  CAS  PubMed  PubMed Central  Google Scholar 

Alquezar C, Salado IG, De La Encarnación A, Pérez DI, Moreno F, Gil C, De Munain AL, Martínez A, Martín-Requero Á (2016) Targeting TDP-43 phosphorylation by Casein Kinase-1δ inhibitors: a novel strategy for the treatment of frontotemporal dementia. Mol Neurodegener 11:36. https://doi.org/10.1186/s13024-016-0102-7

Article  CAS  PubMed  PubMed Central  Google Scholar 

Benatar M, Boylan K, Jeromin A, Rutkove SB, Berry J, Atassi N, Bruijn L (2016) ALS biomarkers for therapy development: state of the field and future directions: ALS biomarkers. Muscle Nerve 53:169–182. https://doi.org/10.1002/mus.24979

Article  PubMed  Google Scholar 

Benatar M, Zhang L, Wang L, Granit V, Statland J, Barohn R, Swenson A, Ravits J, Jackson C, Burns TM, Trivedi J, Pioro EP, Caress J, Katz J, McCauley JL, Rademakers R, Malaspina A, Ostrow LW, Wuu J, Hussain S, Cooley A, Li Y, Wallace M, Steele J, Hernandez JP, Medina J, Paredes ME, Manso A, Ravelo N, Levy W, Whitehead P, Zuchner S, Pasnoor M, Jawdat O, Jabari D, Farmakidis C, Glenn M, Dimachkie MM, Herbelin L, Tanui H, Anderson S, Walker M, Liu T, McCally A, Heim A, Currence M, Harness Y, Sieren J, Gibson E, Gutierrez G, Bussey D, Previte R, Kittrell P, Joshi A, Conger A, Hastings D, Caristo I, Marandi M, Carty S, Taylor JP, Wu G, Rampersaud E, Schule R, Blitterswijk MV (2020) Validation of serum neurofilaments as prognostic and potential pharmacodynamic biomarkers for ALS. Neurology 95. https://doi.org/10.1212/WNL.0000000000009559

Brady OA, Meng P, Zheng Y, Mao Y, Hu F (2011) Regulation of TDP-43 aggregation by phosphorylation andp62/SQSTM1: regulation of TDP-43 aggregation by phosphorylation and p62. J Neurochem 116:248–259. https://doi.org/10.1111/j.1471-4159.2010.07098.x

Article  CAS  PubMed  Google Scholar 

Brown RH, Al-Chalabi A (2017) Amyotrophic lateral sclerosis. N Engl J Med 377:162–172. https://doi.org/10.1056/NEJMra1603471

Article  CAS  PubMed  Google Scholar 

Buratti E (2018) TDP-43 post-translational modifications in health and disease. Expert Opin Ther Targets 22:279–293. https://doi.org/10.1080/14728222.2018.1439923

Article  CAS  PubMed  Google Scholar 

Cheong JK, Virshup DM (2011) Casein kinase 1: complexity in the family. Int J Biochem Cell Biol 43:465–469. https://doi.org/10.1016/j.biocel.2010.12.004

Article  CAS  PubMed  Google Scholar 

Choksi DK, Roy B, Chatterjee S, Yusuff T, Bakhoum MF, Sengupta U, Ambegaokar S, Kayed R, Jackson GR (2014) TDP-43 phosphorylation by casein kinase Iε promotes oligomerization and enhances toxicity in vivo. Hum Mol Genet 23:1025–1035. https://doi.org/10.1093/hmg/ddt498

Article  CAS  PubMed  Google Scholar 

Dormann D, Capell A, Carlson AM, Shankaran SS, Rodde R, Neumann M, Kremmer E, Matsuwaki T, Yamanouchi K, Nishihara M, Haass C (2009) Proteolytic processing of TAR DNA binding protein-43 by caspases produces C‐terminal fragments with disease defining properties independent of progranulin. J Neurochem 110:1082–1094. https://doi.org/10.1111/j.1471-4159.2009.06211.x

Article  CAS  PubMed  Google Scholar 

Etchegaray J-P, Machida KK, Noton E, Constance CM, Dallmann R, Di Napoli MN, DeBruyne JP, Lambert CM, Yu EA, Reppert SM, Weaver DR (2009) Casein Kinase 1 Delta regulates the Pace of the mammalian circadian clock. Mol Cell Biol 29:3853–3866. https://doi.org/10.1128/MCB.00338-09

Article  CAS  PubMed  PubMed Central  Google Scholar 

Fish KJ, Cegielska A, Getman ME, Landes GM, Virshup DM (1995) Isolation and characterization of human casein kinase I∊ (CKI), a Novel Member of the CKI Gene Family. J Biol Chem 270:14875–14883. https://doi.org/10.1074/jbc.270.25.14875

Article  CAS  PubMed  Google Scholar 

Fulcher LJ, Sapkota GP (2020) Functions and regulation of the serine/threonine protein kinase CK1 family: moving beyond promiscuity. Biochem J 477:4603–4621. https://doi.org/10.1042/BCJ20200506

Article  CAS  PubMed  Google Scholar 

Gasset-Rosa F, Lu S, Yu H, Chen C, Melamed Z, Guo L, Shorter J, Da Cruz S, Cleveland DW (2019) Cytoplasmic TDP-43 de-mixing independent of stress granules drives inhibition of Nuclear Import, loss of Nuclear TDP-43, and cell death. Neuron 102:339–357e7. https://doi.org/10.1016/j.neuron.2019.02.038

Article  CAS  PubMed  PubMed Central  Google Scholar 

Gruijs Da Silva LA, Simonetti F, Hutten S, Riemenschneider H, Sternburg EL, Pietrek LM, Gebel J, Dötsch V, Edbauer D, Hummer G, Stelzl LS, Dormann D (2022) Disease-linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation. EMBO J 41:e108443. https://doi.org/10.15252/embj.2021108443

Article  CAS  PubMed  PubMed Central  Google Scholar 

Hasegawa M, Arai T, Nonaka T, Kametani F, Yoshida M, Hashizume Y, Beach TG, Buratti E, Baralle F, Morita M, Nakano I, Oda T, Tsuchiya K, Akiyama H (2008) Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann Neurol 64:60–70. https://doi.org/10.1002/ana.21425

Article  CAS  PubMed  PubMed Central  Google Scholar 

Hasegawa M, Nonaka T, Tsuji H, Tamaoka A, Yamashita M, Kametani F, Yoshida M, Arai T, Akiyama H (2011) Molecular dissection of TDP-43 proteinopathies. J Mol Neurosci 45:480–485. https://doi.org/10.1007/s12031-011-9571-x

Article  CAS  PubMed  Google Scholar 

Hicks DA, Cross LL, Williamson R, Rattray M (2020) Endoplasmic reticulum stress signalling induces casein kinase 1-Dependent formation of cytosolic TDP-43 inclusions in Motor Neuron-Like cells. Neurochem Res 45:1354–1364. https://doi.org/10.1007/s11064-019-02832-2

Article  CAS  PubMed  Google Scholar 

Igaz LM, Kwong LK, Lee EB, Chen-Plotkin A, Swanson E, Unger T, Malunda J, Xu Y, Winton MJ, Trojanowski JQ, Lee VM-Y (2011) Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice. J Clin Invest 121:726–738. https://doi.org/10.1172/JCI44867

Article  CAS  PubMed  PubMed Central  Google Scholar 

Iguchi Y, Katsuno M, Takagi S, Ishigaki S, Niwa J, Hasegawa M, Tanaka F, Sobue G (2012) Oxidative stress induced by glutathione depletion reproduces pathological modifications of TDP-43 linked to TDP-43 proteinopathies. Neurobiol Dis 45:862–870. https://doi.org/10.1016/j.nbd.2011.12.002

Article  CAS  PubMed  Google Scholar 

Inukai Y, Nonaka T, Arai T, Yoshida M, Hashizume Y, Beach TG, Buratti E, Baralle FE, Akiyama H, Hisanaga S, Hasegawa M (2008) Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD‐U and ALS. FEBS Lett 582:2899–2904. https://doi.org/10.1016/j.febslet.2008.07.027

Article  CAS  PubMed  Google Scholar 

Kametani F, Obi T, Shishido T, Akatsu H, Murayama S, Saito Y, Yoshida M, Hasegawa M (2016) Mass spectrometric analysis of accumulated TDP-43 in amyotrophic lateral sclerosis brains. Sci Rep 6:23281. https://doi.org/10.1038/srep23281

Article  CAS  PubMed  PubMed Central  Google Scholar 

Kim KY, Lee H-W, Shim Y, Mook-Jung I, Jeon GS, Sung J-J (2015) A phosphomimetic mutant TDP-43 (S409/410E) induces Drosha instability and cytotoxicity in Neuro 2A cells. Biochem Biophys Res Commun 464:236–243. https://doi.org/10.1016/j.bbrc.2015.06.125

Article  CAS  PubMed  Google Scholar 

Kishino Y, Matsukawa K, Matsumoto T, Miyazaki R, Wakabayashi T, Nonaka T, Kametani F, Hasegawa M, Hashimoto T, Iwatsubo T (2022) Casein kinase 1δ/ε phosphorylates fused in sarcoma (FUS) and ameliorates FUS-mediated neurodegeneration. J Biol Chem 298:102191. https://doi.org/10.1016/j.jbc.2022.102191

Article  CAS  PubMed  PubMed Central  Google Scholar 

Ko VI, Ong K, Cleveland DW, Yu H, Ravits JM (2024) CK1δ/ε kinases regulate TDP-43 phosphorylation and are therapeutic targets for ALS-related TDP-43 hyperphosphorylation. Neurobiol Dis 196:106516. https://doi.org/10.1016/j.nbd.2024.106516