Journal
FEBS LETTERS
Volume 586, Issue 16, Pages 2488-2493Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2012.06.011
Keywords
Gp78; E3 ubiquitin ligase; ERAD; S-palmitoylation; Trafficking; Endoplasmic reticulum
Funding
- Canadian Institutes for Health Research (CIHR) [MT-15132]
- Michael Smith Foundation for Health Research Scholarship
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Gp78 is an E3 ubiquitin ligase within the endoplasmic reticulum-associated degradation pathway. We show that Flag-tagged gp78 undergoes sulfhydryl cysteine palmitoylation (S-palmitoylation) within the RING finger motif, responsible for its ubiquitin ligase activity. Screening of 19 palmitoyl acyl transferases (PATs) identified five that increased gp78 RING finger palmitoylation. Endoplasmic reticulum (ER)-localized Myc-DHHC6 overexpression promoted the peripheral ER distribution of Flag-gp78 while RING finger mutation and the palmitoylation inhibitor 2-bromopalmitate restricted gp78 to the central ER. Palmitoylation of RING finger cysteines therefore regulates gp78 distribution to the peripheral ER. (c) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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