The ER retention protein RER1 promotes alpha-synuclein degradation via the proteasome.
Abnormal accumulation of α-synuclein (αSyn) has been linked to endoplasmic-reticulum (ER) stress, defective intracellular protein/vesicle trafficking, and cytotoxicity. Targeting factors involved in ER-related protein processing and trafficking may, therefore, be a key to modulating αSyn levels and...
Saved in:
| Main Authors: | Hyo-Jin Park, Daniel Ryu, Mayur Parmar, Benoit I Giasson, Nikolaus R McFarland |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2017-01-01
|
| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0184262&type=printable |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Aspirin inhibits proteasomal degradation and promotes α-synuclein aggregate clearance through K63 ubiquitination
by: Jing Gao, et al.
Published: (2025-02-01) -
The role of alpha-synuclein in synucleinopathy: Impact on lipid regulation at mitochondria–ER membranes
by: Peter A. Barbuti, et al.
Published: (2025-04-01) -
Parkinson’s paradox: alpha-synuclein’s selective strike on SNc dopamine neurons over VTA
by: L. Phan, et al.
Published: (2025-07-01) -
A territorial development project associated with the Brussels RER
by: Patrick Frenay
Published: (2009-11-01) -
RER1 regulates lipid metabolism in monocytes and macrophages
by: Yanxia Liu, et al.
Published: (2025-08-01)