TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum
TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum
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DOI：
10.1042/bj20041241
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发表时间：
2005-06-01
影响因子：
4.1
通讯作者：
Wiertz, E
中科院分区：
文献类型：
--
作者：
Hassink, G;Kikkert, M;Wiertz, E
在本研究中，人TEB4被鉴定为一种新的内质网驻留泛素连接酶。TEB4在许多物种中都有同源物，并具有许多显著的性质。TEB4包含一个保守的环(真正有趣的新基因)指和13个预测的跨膜结构域。TEB4及其同系物的环翅位于N-末端，具有非传统的C4HC3构型。TEB4的N-末端位于胞浆中。我们发现，分离的TEB4环区在体外催化泛素连接，反应是泛素赖氨酸(48)特异性的，涉及Ubc7(泛素结合酶7)。这些特性让人想起E3酶，它参与内质网相关蛋白的降解。TEB4本身是一种内质网降解底物，以无名指和蛋白酶体依赖的方式促进自身的降解。
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.