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TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum
被引:143
作者:
Hassink, G
Kikkert, M
van Voorden, S
Lee, SJ
Spaapen, R
van Laar, T
Coleman, CS
Bartee, E
Früh, K
Chau, V
Wiertz, E
机构:
[1] Leiden Univ, Med Ctr, Dept Med Microbiol, NL-2300 RC Leiden, Netherlands
[2] Natl Hlth Res Inst, Div Biotechnol & Pharmaceut Res, Taipei 114, Taiwan
[3] Netherlands Canc Inst, Div Mol Genet, NL-1066 CX Amsterdam, Netherlands
[4] Penn State Univ, Coll Med, Milton S Hershey Med Ctr, Dept Cellular & Mol Physiol, Hershey, PA 17033 USA
[5] Oregon Hlth & Sci Univ, Vaccine & Gene Therapy Inst, Beaverton, OR 97006 USA
关键词:
E3 ubiquitin protein ligase;
endoplasmic reticulum-associated degradation;
proteasome;
RING finger;
TEB4;
ubiquitin;
D O I:
10.1042/BJ20041241
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
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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页码:647 / 655
页数:9
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