The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum
Open accessAbstract
In the present study, the human TEB4 is identified as a novel ER (endoplasmic reticulum)-resident ubiquitin ligase. TEB4 has homologues in many species and has a number of remarkable properties. TEB4 contains a conserved RING (really interesting new gene) finger and 13 predicted transmembrane domains. The RING finger of TEB4 and its homologues is situated at the N-terminus and has the unconventional C4HC3 configuration. The N-terminus of TEB4 is located in the cytosol. We show that the isolated TEB4 RING domain catalyses ubiquitin ligation in vitro in a reaction that is ubiquitin Lys48-specific and involves UBC7 (ubiquitin-conjugating enzyme 7). These properties are reminiscent of E3 enzymes, which are involved in ER-associated protein degradation. TEB4 is an ER degradation substrate itself, promoting its own degradation in a RING finger- and proteasome-dependent manner.
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Cites
A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., & Varshavsky, A. (1989) · Science · doi:10.1126/science.2538923 · Cited by 1,535
Self-citationKikkert, M., Doolman, R., Dai, M., Avner, R., Hassink, G., van Voorden, S., Thanedar, S., Roitelman, J., Chau, V., & Wiertz, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307453200 · Cited by 384
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Cited by
One step at a time: endoplasmic reticulum-associated degradation
Vembar, S. S., & Brodsky, J. L. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2546 · Cited by 1,299
Cellular and Molecular Basis of Deiodinase-Regulated Thyroid Hormone Signaling1
Gereben, B., Zavacki, A. M., Ribich, S., Kim, B. W., Huang, S. A., Simonides, W. S., Zeöld, A., & Bianco, A. C. (2008) · Endocrine Reviews · doi:10.1210/er.2008-0019 · Cited by 891
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
Li, Y., Li, S., & Wu, H. (2022) · Cells · doi:10.3390/cells11050851 · Cited by 367
The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation
Weissman, A. M., Shabek, N., & Ciechanover, A. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3173 · Cited by 317
Metadata
- Authors
- HASSINK, G., KIKKERT, M., VOORDEN, S. V., LEE, S.-J., SPAAPEN, R., LAAR, T. V., COLEMAN, C. S., BARTEE, E., FRÜH, K., CHAU, V., & WIERTZ, E.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2005-05-24
- Volume
- 388
- Issue
- 2
- Pages
- 647-655
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W2029119458
- Cited by
- 172
- References
- 2
- FWCI
- 4.84
- Type
- journal article
- Language
- en
- Open access
- bronze
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- HASSINK, G., KIKKERT, M., VOORDEN, S. V., LEE, S.-J., SPAAPEN, R., LAAR, T. V., COLEMAN, C. S., BARTEE, E., FRÜH, K., CHAU, V., & WIERTZ, E. (2005). TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum. Biochemical Journal. https://doi.org/10.1042/bj20041241
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