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gp78: a Multifaceted Ubiquitin Ligase that Integrates a Unique Protein Degradation Pathway from the Endoplasmic Reticulum
- Source :
- Current Protein & Peptide Science. 13:414-424
- Publication Year :
- 2012
- Publisher :
- Bentham Science Publishers Ltd., 2012.
-
Abstract
- The endoplasmic reticulum (ER) is the site for maturation of proteins destined for the secretory pathway. Failure in maturation leads to production of misfolded proteins that are eliminated through the ER-associated degradation (ERAD) pathway. ERAD is a complex process that includes misfolded protein recognition, retrotranslocation to the cytosol, ubiquitination and proteasomal degradation. gp78 is an E3 ubiquitin ligase that integrates these ERAD steps by nucleating a unique degradation machine, which uses the p97/VCP-Npl4 complex for retrotranslocation instead of the wellknown p97/VCP-Ufd1-Npl4 complex. A growing list of substrates have been identified for gp78, which highlights the importance of gp78-mediated ERAD in essential physiological pathways and pathological processes.
- Subjects :
- Molecular Sequence Data
macromolecular substances
Endoplasmic-reticulum-associated protein degradation
Protein degradation
Endoplasmic Reticulum
Biochemistry
Ubiquitin
Animals
Humans
Amino Acid Sequence
Molecular Biology
Secretory pathway
biology
Endoplasmic reticulum
Ubiquitination
Neurodegenerative Diseases
Cell Biology
General Medicine
Ubiquitin ligase
Cell biology
Receptors, Autocrine Motility Factor
Proteolysis
biology.protein
Protein folding
Signal transduction
Sequence Alignment
Signal Transduction
Subjects
Details
- ISSN :
- 13892037
- Volume :
- 13
- Database :
- OpenAIRE
- Journal :
- Current Protein & Peptide Science
- Accession number :
- edsair.doi.dedup.....e50b717db8f892f7df96933c65a38b6f