| First Author | Fairbank M | Year | 2012 |
| Journal | FEBS Lett | Volume | 586 |
| Issue | 16 | Pages | 2488-93 |
| PubMed ID | 22728137 | Mgi Jnum | J:186415 |
| Mgi Id | MGI:5432290 | Doi | 10.1016/j.febslet.2012.06.011 |
| Citation | Fairbank M, et al. (2012) RING finger palmitoylation of the endoplasmic reticulum Gp78 E3 ubiquitin ligase. FEBS Lett 586(16):2488-93 |
| abstractText | 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. |
