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TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum
Copyright policy )TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum
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.
- Pennsylvania State University United States
- Antoni van Leeuwenhoek Hospital Netherlands
- Leiden University Medical Center Netherlands
- Oregon Health & Science University United States
- Penn State Milton S. Hershey Medical Center United States
Microsoft Academic Graph classification: Endoplasmic-reticulum-associated protein degradation Protein degradation Ubiquitin-conjugating enzyme Ubiquitin Ring finger medicine biology Chemistry Endoplasmic reticulum STIM1 Ubiquitin ligase medicine.anatomical_structure Biochemistry biology.protein
Ubiquitin-Protein Ligases, Molecular Sequence Data, Endoplasmic Reticulum, Biochemistry, Amino Acid Sequence, Molecular Biology, Sequence Homology, Amino Acid, Ubiquitin, Membrane Proteins, Zinc Fingers, Cell Biology, Ubiquitin-Conjugating Enzymes, Sequence Alignment, Research Article, Protein Binding
Ubiquitin-Protein Ligases, Molecular Sequence Data, Endoplasmic Reticulum, Biochemistry, Amino Acid Sequence, Molecular Biology, Sequence Homology, Amino Acid, Ubiquitin, Membrane Proteins, Zinc Fingers, Cell Biology, Ubiquitin-Conjugating Enzymes, Sequence Alignment, Research Article, Protein Binding
Microsoft Academic Graph classification: Endoplasmic-reticulum-associated protein degradation Protein degradation Ubiquitin-conjugating enzyme Ubiquitin Ring finger medicine biology Chemistry Endoplasmic reticulum STIM1 Ubiquitin ligase medicine.anatomical_structure Biochemistry biology.protein
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).139 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 10% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 1% citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).139 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 10% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 1%
Citations provided by BIP!Popularity provided by BIP!- Pennsylvania State University United States
- Antoni van Leeuwenhoek Hospital Netherlands
- Leiden University Medical Center Netherlands
- Oregon Health & Science University United States
- Penn State Milton S. Hershey Medical Center United States
- National Health Research Institutes Taiwan
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.