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A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
A p97-interacting membrane protein complex in the mammalian ER that links elimination of misfolded proteins from the endoplasmic reticulum by retro-translocation and its subsequent movement through the membrane by the cytosolic p97 ATPase is identified.
The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
This work proposes that the Cdc48/p97–Ufd1–Npl4 complex extracts proteins from the ER membrane for cytosolic degradation, and demonstrates that it requires the interacting partners Ufd1 and Npl4.
Building ubiquitin chains: E2 enzymes at work
The E2s are able to govern the switch from ubiquitin chain initiation to elongation, regulate the processivity of chain formation and establish the topology of assembled chains, thereby determining the consequences of ubiquitylation for the modified proteins.
Function of the p97–Ufd1–Npl4 complex in retrotranslocation from the ER to the cytosol
A dual recognition model is proposed in which the p97–Ufd1–Npl4 complex binds both a nonmodified segment of the substrate and the attached polyubiquitin chain; polyubanquitin binding may activate the ATPase p97 to pull the polypeptide substrate out of the membrane.
Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
- Billy Tsai, Y. Ye, T. Rapoport
- Biology, Computer ScienceNature Reviews Molecular Cell Biology
- 1 April 2002
The mechanism of retro-translocation is still mysterious, but several aspects of this process are now being unravelled.
Cleaning up in the endoplasmic reticulum: ubiquitin in charge
The eukaryotic endoplasmic reticulum (ER) maintains protein homeostasis by eliminating unwanted proteins through the evolutionarily conserved ER-associated degradation (ERAD) pathway and the ubiquitin system is functionally intertwined with retrotranslocation machinery to transport polypeptides across the ER membrane.
ERAD inhibitors integrate ER stress with an epigenetic mechanism to activate BH3-only protein NOXA in cancer cells
- Qiuyan Wang, H. Mora-Jensen, Y. Ye
- BiologyProceedings of the National Academy of Sciences
- 17 February 2009
Eeyarestatin I (EerI), a chemical inhibitor that blocks endoplasmic reticulum (ER)-associated protein degradation, has antitumor and biologic activities similar to bortezomib and can synergize with bortzomib, which identifies a class of anticancer agents that integrate ER stress response with an epigenetic mechanism to induce cell death.
Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants
It is shown that presenilin is required for the normal proteolytic production of carboxy-terminal Notch fragments that are needed for receptor maturation and signalling, and that genetically it acts upstream of both the membrane-bound form and the activated nuclear form of Notch.
Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase.
- Y. Ye
- BiologyJournal of structural biology
- 1 October 2006
A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate
It is demonstrated by expressing recombinant proteins in Escherichia coli that Ube2g2/gp78-mediated polyubiquitination involves preassembly of Lys 48-linked ubiquitin chains at the catalytic cysteine of Ube 2g2.