國家衛生研究院 NHRI:Item 3990099045/1117
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    Please use this identifier to cite or link to this item: http://ir.nhri.org.tw/handle/3990099045/1117


    Title: TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum
    Authors: Hassink, G;Kikkert, M;van Voorden, S;Lee, SJ;Spaapen, R;van Laar, T;Coleman, CS;Bartee, E;Fruh, K;Chau, V;Wiertz, E
    Contributors: Division of Biotechnology and Pharmaceutical Research
    Abstract: 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.
    Keywords: Biochemistry & Molecular Biology
    Date: 2005-06-01
    Relation: Biochemical Journal. 2005 Jun;388(Pt. 2):647-655.
    Link to: http://dx.doi.org/10.1042/BJ20041241
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=0264-6021&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000229919500028
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=20544440605
    Appears in Collections:[Shiow-Ju Lee] Periodical Articles

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