The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
ENDOPLASMIC RETICULUM–ASSOCIATED DEGRADATION
Abstract
Secretory and transmembrane proteins enter the secretory pathway through the protein-conducting Sec61 channel in the membrane of the endoplasmic reticulum. In the endoplasmic reticulum, proteins fold, are frequently covalently modified, and oligomerize before they are packaged into transport vesicles that shuttle them to the Golgi complex. Proteins that misfold in the endoplasmic reticulum are selectively transported back across the endoplasmic reticulum membrane to the cytosol for degradation by proteasomes. Depending on the topology of the defect in the protein, cytosolic or lumenal chaperones are involved in its targeting to degradation. The export channel for misfolded proteins is likely also formed by Sec61p. Export may be powered by AAA-ATPases of the proteasome 19S regulatory particle or Cdc48p/p97. Exported proteins are frequently ubiquitylated prior to degradation and are escorted to the proteasome by polyubiquitin-binding proteins.
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Cites
Protein degradation and protection against misfolded or damaged proteins.
Goldberg, A. L. (2003) · Nature · doi:10.1038/nature02263 · Cited by 2,088
Roles of N-Linked Glycans in the Endoplasmic Reticulum
Helenius, A., & Aebi, M. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073752 · Cited by 2,037
The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
Ye, Y., Meyer, H. H., & Rapoport, T. A. (2001) · Nature · doi:10.1038/414652a · Cited by 1,099
Cited by
Autophagy Counterbalances Endoplasmic Reticulum Expansion during the Unfolded Protein Response
Bernales, S., McDonald, K. L., & Walter, P. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040423 · Cited by 1,007
A Luminal Surveillance Complex that Selects Misfolded Glycoproteins for ER-Associated Degradation
Denic, V., Quan, E. M., & Weissman, J. S. (2006) · Cell · doi:10.1016/j.cell.2006.05.045 · Cited by 422
HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination
Boyault, C., Sadoul, K., Pabion, M., & Khochbin, S. (2007) · Oncogene · doi:10.1038/sj.onc.1210614 · Cited by 397
N-glycan structure dictates extension of protein folding or onset of disposal
Molinari, M. (2007) · Nature Chemical Biology · doi:10.1038/nchembio880 · Cited by 300
A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum
Ploegh, H. L. (2007) · Nature · doi:10.1038/nature06004 · Cited by 283
Metadata
- Authors
- Römisch, K.
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2005-11-01
- Volume
- 21
- Issue
- 1
- Pages
- 435-456
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2135513925
- Cited by
- 365
- References
- 3
- FWCI
- 2.40
- Type
- journal article
- Language
- en
- Open access
- closed
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- Römisch, K. (2005). ENDOPLASMIC RETICULUM–ASSOCIATED DEGRADATION. Annual Review of Cell and Developmental Biology. https://doi.org/10.1146/annurev.cellbio.21.012704.133250
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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