Acetylation of N-terminus and two internal amino acids is dispensable for degradation of a protein that aberrantly engages the endoplasmic reticulum translocon

Acetylation of N-terminus and two internal amino acids is dispensable for degradation of a protein that aberrantly engages the endoplasmic reticulum translocon

Conserved homologues of the Hrd1 ubiquitin ligase target for degradation proteins that persistently or aberrantly engage the endoplasmic reticulum translocon, including mammalian apolipoprotein B (apoB; the major protein component of low-density lipoproteins) and the artificial yeast protein Deg1-Se...

Full description

Bibliographic Details
Main Authors: Sarah M. Engle, Justin J. Crowder, Sheldon G. Watts, Christopher J. Indovina, Samuel Z. Coffey, Eric M. Rubenstein
Format: Article
Language:English
Published: PeerJ Inc. 2017-08-01
Series:PeerJ
Subjects:
Acetylation
Apolipoprotein B
Nat3
Translocon
Protein quality control
Protein degradation
Online Access:https://peerj.com/articles/3728.pdf

Internet

https://peerj.com/articles/3728.pdf

Similar Items