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Dysregulation of the progranulin-driven autophagy-lysosomal pathway mediates secretion of the nuclear protein TDP-43.
Tanaka, Yoshinori; Ito, Shun-Ichi; Honma, Yuki; Hasegawa, Masato; Kametani, Fuyuki; Suzuki, Genjiro; Kozuma, Lina; Takeya, Kosuke; Eto, Masumi.
  • Tanaka Y; Biochemistry Unit, Faculty of Veterinary Medicine, Okayama University of Science, Imabari-shi, Ehime, Japan. Electronic address: y-tanaka@ous.ac.jp.
  • Ito SI; Biochemistry Unit, Faculty of Veterinary Medicine, Okayama University of Science, Imabari-shi, Ehime, Japan.
  • Honma Y; Biochemistry Unit, Faculty of Veterinary Medicine, Okayama University of Science, Imabari-shi, Ehime, Japan.
  • Hasegawa M; Department of Brain and Neurosciences, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
  • Kametani F; Department of Brain and Neurosciences, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
  • Suzuki G; Department of Brain and Neurosciences, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
  • Kozuma L; Biochemistry Unit, Faculty of Veterinary Medicine, Okayama University of Science, Imabari-shi, Ehime, Japan.
  • Takeya K; Biochemistry Unit, Faculty of Veterinary Medicine, Okayama University of Science, Imabari-shi, Ehime, Japan.
  • Eto M; Biochemistry Unit, Faculty of Veterinary Medicine, Okayama University of Science, Imabari-shi, Ehime, Japan.
J Biol Chem ; 299(11): 105272, 2023 11.
Article en En | MEDLINE | ID: mdl-37739033
The cytoplasmic accumulation of the nuclear protein transactive response DNA-binding protein 43 kDa (TDP-43) has been linked to the progression of amyotrophic lateral sclerosis and frontotemporal lobar degeneration. TDP-43 secreted into the extracellular space has been suggested to contribute to the cell-to-cell spread of the cytoplasmic accumulation of TDP-43 throughout the brain; however, the underlying mechanisms remain unknown. We herein demonstrated that the secretion of TDP-43 was stimulated by the inhibition of the autophagy-lysosomal pathway driven by progranulin (PGRN), a causal protein of frontotemporal lobar degeneration. Among modulators of autophagy, only vacuolar-ATPase inhibitors, such as bafilomycin A1 (Baf), increased the levels of the full-length and cleaved forms of TDP-43 and the autophagosome marker LC3-II (microtubule-associated proteins 1A/1B light chain 3B) in extracellular vesicle fractions prepared from the culture media of HeLa, SH-SY5Y, or NSC-34 cells, whereas vacuolin-1, MG132, chloroquine, rapamycin, and serum starvation did not. The C-terminal fragment of TDP-43 was required for Baf-induced TDP-43 secretion. The Baf treatment induced the translocation of the aggregate-prone GFP-tagged C-terminal fragment of TDP-43 and mCherry-tagged LC3 to the plasma membrane. The Baf-induced secretion of TDP-43 was attenuated in autophagy-deficient ATG16L1 knockout HeLa cells. The knockdown of PGRN induced the secretion of cleaved TDP-43 in an autophagy-dependent manner in HeLa cells. The KO of PGRN in mouse embryonic fibroblasts increased the secretion of the cleaved forms of TDP-43 and LC3-II. The treatment inducing TDP-43 secretion increased the nuclear translocation of GFP-tagged transcription factor EB, a master regulator of the autophagy-lysosomal pathway in SH-SY5Y cells. These results suggest that the secretion of TDP-43 is promoted by dysregulation of the PGRN-driven autophagy-lysosomal pathway.
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Autofagia / Proteínas de Unión al ADN / Progranulinas / Lisosomas Límite: Humans Idioma: En Año: 2023 Tipo del documento: Article

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Autofagia / Proteínas de Unión al ADN / Progranulinas / Lisosomas Límite: Humans Idioma: En Año: 2023 Tipo del documento: Article