TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum

Gerco Hassink; Marjolein Kikkert; Sjaak Van Voorden; Shiow Ju Lee; Robbert Spaapen; Theo Van Laar; Catherine S. Coleman; Eric Bartee; Klaus Früh; Vincent Chau; Emmanuel Wiertz

doi:10.1042/BJ20041241

TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum

Gerco Hassink, Marjolein Kikkert, Sjaak Van Voorden, Shiow Ju Lee, Robbert Spaapen, Theo Van Laar, Catherine S. Coleman, Eric Bartee, Klaus Früh, Vincent Chau, Emmanuel Wiertz

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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 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 Lys ⁴⁸-specific and involves UBC7 (ubiguitin-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.

Original language	English (US)
Pages (from-to)	647-655
Number of pages	9
Journal	Biochemical Journal
Volume	388
Issue number	2
DOIs	https://doi.org/10.1042/BJ20041241
State	Published - Jun 1 2005

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

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10.1042/BJ20041241

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title = "TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum",

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 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 Lys 48-specific and involves UBC7 (ubiguitin-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.",

author = "Gerco Hassink and Marjolein Kikkert and {Van Voorden}, Sjaak and Lee, {Shiow Ju} and Robbert Spaapen and {Van Laar}, Theo and Coleman, {Catherine S.} and Eric Bartee and Klaus Fr{\"u}h and Vincent Chau and Emmanuel Wiertz",

year = "2005",

month = jun,

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doi = "10.1042/BJ20041241",

language = "English (US)",

volume = "388",

pages = "647--655",

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T1 - TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum

AU - Hassink, Gerco

AU - Kikkert, Marjolein

AU - Van Voorden, Sjaak

AU - Lee, Shiow Ju

AU - Spaapen, Robbert

AU - Van Laar, Theo

AU - Coleman, Catherine S.

AU - Bartee, Eric

AU - Früh, Klaus

AU - Chau, Vincent

AU - Wiertz, Emmanuel

PY - 2005/6/1

Y1 - 2005/6/1

N2 - 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 Lys 48-specific and involves UBC7 (ubiguitin-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.

AB - 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 Lys 48-specific and involves UBC7 (ubiguitin-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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JO - Biochemical Journal

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TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum

Abstract

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