The tissue-specific Rep8/UBXD6 tethers p97 to the endoplasmic reticulum membrane for degradation of misfolded proteins.
The protein known as p97 or VCP in mammals and Cdc48 in yeast is a versatile ATPase complex involved in several biological functions including membrane fusion, protein folding, and activation of membrane-bound transcription factors. In addition, p97 plays a central role in degradation of misfolded s...
Saved in:
| Main Authors: | Louise Madsen, Franziska Kriegenburg, Andrea Vala, Diana Best, Søren Prag, Kay Hofmann, Michael Seeger, Ian R Adams, Rasmus Hartmann-Petersen |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2011-01-01
|
| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0025061&type=printable |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Stress Management: How the Endoplasmic Reticulum Mitigates Protein Misfolding and Oxidative Stress by the Dual Role of Glutathione Peroxidase 8
by: Yong Yang, et al.
Published: (2025-06-01) -
Membrane-tethered SCOTIN condensates elicit an endoplasmic reticulum stress response by sequestering luminal BiP
by: Areum Jo, et al.
Published: (2025-02-01) -
Erratum to “Not so Rare: Diseases based on Mutant Proteins Controlling Endoplasmic Reticulum-Mitochondria Contact (MERC) Tethering”
Published: (2024-09-01) -
Endoplasmic Reticulum Stress in Cancer
by: Ruixin Zhou, et al.
Published: (2025-07-01) -
Endoplasmic Reticulum Stress and Lipid Metabolism
by: Huiping Zhou, et al.
Published: (2012-01-01)