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FEBS Lett. 2012 Jul 30;586(16):2488-93. doi: 10.1016/j.febslet.2012.06.011. Epub 2012 Jun 21.

RING finger palmitoylation of the endoplasmic reticulum Gp78 E3 ubiquitin ligase.

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1
University of British Columbia, Department of Cellular and Physiological Sciences, Vancouver, British Columbia, Canada.

Abstract

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.

PMID:
22728137
DOI:
10.1016/j.febslet.2012.06.011
[Indexed for MEDLINE]
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