RING finger palmitoylation of the endoplasmic reticulum Gp78 E3 ubiquitin ligase

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


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Binding Sites
  • COS Cells
  • Chlorocebus aethiops
  • Endoplasmic Reticulum / metabolism*
  • Gene Expression Regulation
  • Mice
  • Microscopy, Fluorescence / methods
  • Mutation
  • Palmitates / chemistry
  • Palmitic Acids / chemistry
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Structure, Tertiary
  • Protein Transport
  • Receptors, Autocrine Motility Factor / chemistry*


  • Palmitates
  • Palmitic Acids
  • 2-bromopalmitate
  • Amfr protein, mouse
  • Receptors, Autocrine Motility Factor
  • Proteasome Endopeptidase Complex