The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matα2 repressor degradation
Open accessAbstract
Substrate discrimination in the ubiquitin–proteasome system is believed to be dictated by specific combinations of ubiquitin–protein ligases (E3s) and ubiquitin-conjugating enzymes (E2s). Here we identify Doa10/Ssm4 as a yeast E3 that is embedded in the endoplasmic reticulum (ER)/nuclear envelope yet can target the soluble transcription factor Matα2. Doa10 contains an unusual RING finger, which has ubiquitin-ligase activity in vitro and is essential in vivo for degradation of α2 via its Deg1 degradation signal. Doa10 functions with two E2s, Ubc6 and Ubc7, to ubiquitinate Deg1 -bearing substrates, and it is also required for the degradation of at least one ER membrane protein. Interestingly, different short-lived ER proteins show distinct requirements for Doa10 and another ER-localized E3, Hrd1. Nevertheless, the two E3s overlap in function: A doa10 Δ hrd1 Δ mutant is far more sensitive to cadmium relative to either single mutant and displays strong constitutive induction of the unfolded protein response; this suggests a role for both E3s in eliminating aberrant ER proteins. The likely human ortholog of DOA10 is in the cri-du-chat syndrome critical region on chromosome 5p, suggesting that defective ubiquitin ligation might contribute to this common genetic disorder.
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Cited by
Modification of Proteins by Ubiquitin and Ubiquitin-Like Proteins
Kerscher, O., Felberbaum, R., & Hochstrasser, M. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010605.093503 · Cited by 1,517
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N-Terminal Acetylation of Cellular Proteins Creates Specific Degradation Signals
Hwang, C.-S., Shemorry, A., & Varshavsky, A. (2010) · Science · doi:10.1126/science.1183147 · Cited by 650
HECT and RING finger families of E3 ubiquitin ligases at a glance
Metzger, M. B., Hristova, V. A., & Weissman, A. M. (2012) · Journal of Cell Science · doi:10.1242/jcs.091777 · Cited by 630
ER-associated degradation: Protein quality control and beyond
Ruggiano, A., Foresti, O., & Carvalho, P. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201312042 · Cited by 607
Metadata
- Authors
- Swanson, R., Locher, M., & Hochstrasser, M.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2001-10-15
- Volume
- 15
- Issue
- 20
- Pages
- 2660-2674
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2146183177
- Cited by
- 455
- References
- 43
- Type
- posted content
- Language
- en
- Open access
- diamond
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- Swanson, R., Locher, M., & Hochstrasser, M. (2001). A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matα2 repressor degradation. Genes & Development. https://doi.org/10.1101/gad.933301
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