The role of the ubiquitination machinery in dislocation and degradation of endoplasmic reticulum proteins

M. Kikkert*, G. Hassink, E. Wiertz

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

6 Citations (Scopus)

Abstract

Ubiquitination is essential for the dislocation and degradation of proteins from the endoplasmic reticulum (ER). How exactly this is regulated is unknown at present. This review provides an overview of ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s) with a role in the degradation of ER proteins. Their structure and functions are described, as well as their mutual interactions. Substrate specificity and functional redundancy of E3 ligases are discussed, and other components of the ER degradation machinery that may associate with the ubiquitination system are reviewed.

Original languageEnglish
Title of host publicationDislocation and Degradation of Proteins from the Endoplasmic Reticulum
EditorsEmmanuel Wiertz, Marjolein Kikkert
PublisherSpringer
Pages57-93
Number of pages37
ISBN (Electronic)978-3-540-28007-1
ISBN (Print)978-3-540-28006-4
DOIs
Publication statusPublished - 2006
Externally publishedYes

Publication series

NameCurrent Topics in Microbiology and Immunology
PublisherSpringer
Volume300
ISSN (Print)0070-217X

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