Journal
BIOCHEMICAL JOURNAL
Volume 388, Issue -, Pages 647-655Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20041241
Keywords
E3 ubiquitin protein ligase; endoplasmic reticulum-associated degradation; proteasome; RING finger; TEB4; ubiquitin
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Funding
- NIGMS NIH HHS [R01 GM062194, GM062194] Funding Source: Medline
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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 fin-er 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 Lys(48)-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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