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

doi:10.1016/j.febslet.2012.06.011

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

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

FEBS letters - 30 Jul 2012

Fairbank Maria, Huang Kun, El-Husseini Alaa, Nabi Ivan R

Abstract excerpt

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...

Topics

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

Source

Open in PubMed

Identifiers

PMID: 22728137
DOI: 10.1016/j.febslet.2012.06.011

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics