Neurons Export Extracellular Vesicles Enriched in Cysteine String Protein and Misfolded Protein Cargo
Abstract The fidelity of synaptic transmission depends on the integrity of the protein machinery at the synapse. Unfolded synaptic proteins undergo refolding or degradation in order to maintain synaptic proteostasis and preserve synaptic function, and buildup of unfolded/toxic proteins leads to neur...
Saved in:
Main Authors: | Jingti Deng, Carolina Koutras, Julien Donnelier, Mana Alshehri, Maryam Fotouhi, Martine Girard, Steve Casha, Peter S. McPherson, Stephen M. Robbins, Janice E. A. Braun |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2017
|
Subjects: | |
Online Access: | https://doaj.org/article/3828e669537c4a758aa77d1df0d2eb5f |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
A cluster of palmitoylated cysteines are essential for aggregation of cysteine-string protein mutants that cause neuronal ceroid lipofuscinosis
by: Cinta Diez-Ardanuy, et al.
Published: (2017) -
The Cytotoxicity and Clearance of Mutant Huntingtin and Other Misfolded Proteins
by: Austin Folger, et al.
Published: (2021) -
Interplay of buried histidine protonation and protein stability in prion misfolding
by: Anatoly Malevanets, et al.
Published: (2017) -
ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function
by: Adrián Cortés Sanchón, et al.
Published: (2021) -
Glycosaminoglycan sulphation affects the seeded misfolding of a mutant prion protein.
by: Victoria A Lawson, et al.
Published: (2010)