Proteins that fail to correctly fold or assemble into oligomeric complexes in the endoplasmic reticulum (ER) are degraded by a ubiquitin- and proteasome-dependent process known as ER-associated degradation (ERAD). Although many individual components of the ERAD system have been identified, how these proteins are organized into a functional network that coordinates recognition, ubiquitylation and dislocation of substrates across the ER membrane is not well understood. We have investigated the functional organization of the mammalian ERAD system using a systems-level strategy that integrates proteomics, functional genomics and the transcriptional response to ER stress. This analysis supports an adaptive organization for the mammalian ERAD machinery and reveals a number of metazoan-specific genes not previously linked to ERAD.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
Proteins that fail to correctly fold or assemble into oligomeric complexes in the endoplasmic reticulum (ER) are degraded by a ubiquitin- and proteasome-dependent process known as ER-associated degradation (ERAD). Although many individual components of the ERAD system have been identified, how these proteins are organized into a functional network that coordinates recognition, ubiquitylation and dislocation of substrates across the ER membrane is not well understood. We have investigated the functional organization of the mammalian ERAD system using a systems-level strategy that integrates proteomics, functional genomics and the transcriptional response to ER stress. This analysis supports an adaptive organization for the mammalian ERAD machinery and reveals a number of metazoan-specific genes not previously linked to ERAD.
|
| skos:exactMatch | |
| uniprot:name |
Nat. Cell Biol.
|
| uniprot:author |
Bennett E.J.,
Christianson J.C.,
Greenblatt E.J.,
Harper J.W.,
Kopito R.R.,
Olzmann J.A.,
Richter C.M.,
Shaler T.A.,
Sowa M.E.,
Tyler R.E.
|
| uniprot:date |
2012
|
| uniprot:pages |
93-105
|
| uniprot:title |
Defining human ERAD networks through an integrative mapping strategy.
|
| uniprot:volume |
14
|
| dc-term:identifier |
doi:10.1038/ncb2383
|