The role of the ubiquitination machinery in dislocation and degradation of endoplasmic reticulum proteins.
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.
Department of Medical Microbiology, Leiden University Medical Center (LUMC), Albinusdreef 2, 2333 ZA Leiden, The Netherlands. m.kikkert@lumc.nl
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D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006801:Humans; D021381:Protein Transport; D011506:Proteins / Q000378:metabolism*; D060285:Receptors, Autocrine Motility Factor; D018121:Receptors, Cytokine / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000502:physiology; D025801:Ubiquitin / Q000378:metabolism*; D044763:Ubiquitin-Conjugating Enzymes / Q000502:physiology; D044767:Ubiquitin-Protein Ligases / Q000502:physiology
D011506:Proteins; D018121:Receptors, Cytokine; D029701:Saccharomyces cerevisiae Proteins; D025801:Ubiquitin; D044763:Ubiquitin-Conjugating Enzymes; C555000:AMFR protein, human; C104621:HRD1 protein, S cerevisiae; D060285:Receptors, Autocrine Motility Factor; C482345:SYVN1 protein, human; D044767:Ubiquitin-Protein Ligases