Endocytosis regulates TDP-43 toxicity and turnover
Impaired turnover of TDP-43 by impaired autophagy or proteasomal function have been suggested to be the cause of TDP-43 accumulation, a hallmark of ALS. Here the authors demonstrate that endocytosis is also important for regulating TDP-43 turnover and toxicity.
Saved in:
Main Authors: | Guangbo Liu, Alyssa N. Coyne, Fen Pei, Spencer Vaughan, Matthew Chaung, Daniela C. Zarnescu, J. Ross Buchan |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2017
|
Subjects: | |
Online Access: | https://doaj.org/article/fa7506d18b1946d4bf2cfee228a8cc57 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
The cooperative binding of TDP-43 to GU-rich RNA repeats antagonizes TDP-43 aggregation
by: Juan Carlos Rengifo-Gonzalez, et al.
Published: (2021) -
Metals in ALS TDP-43 Pathology
by: Lassi Koski, et al.
Published: (2021) -
Tau-tubulin kinase 1 phosphorylates TDP-43 at disease-relevant sites and exacerbates TDP-43 pathology
by: Yuan Tian, et al.
Published: (2021) -
HEXA-018, a Novel Inducer of Autophagy, Rescues TDP-43 Toxicity in Neuronal Cells
by: Shinrye Lee, et al.
Published: (2021) -
Aberrant activation of non-coding RNA targets of transcriptional elongation complexes contributes to TDP-43 toxicity
by: Chia-Yu Chung, et al.
Published: (2018)