ArticleJournal of cell science2010
Role of intramembrane charged residues in the quality control of unassembled T-cell receptor alpha-chains at the endoplasmic reticulum.
Article in Journal of cell science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- USP13: Multiple Functions and Target Inhibition.Frontiers in cell and developmental biology · 2022Review
- C-terminal tail length guides insertion and assembly of membrane proteins.The Journal of biological chemistry · 2020Article
- The Role of the Small Export Apparatus Protein, SctS, in the Activity of the Type III Secretion System.Frontiers in microbiology · 2019Article
- The Third Transmembrane Domain of EscR Is Critical for Function of the EnteropathogenicmSphere · 2018Article
- The Role of Autophagy in the Degradation of Misfolded HLA-B27 Heavy Chains.Arthritis & rheumatology (Hoboken, N.J.) · 2018Article
- Engineered Cross-Linking to Study the Pore Architecture of the CRAC Channel.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Ubiquilin1 represses migration and epithelial-to-mesenchymal transition of human non-small cell lung cancer cells.Oncogene · 2015Article
- Dimeric Ube2g2 simultaneously engages donor and acceptor ubiquitins to form Lys48-linked ubiquitin chains.The EMBO journal · 2014Article
- USP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradation.eLife · 2014Article
- Orchestration of secretory protein folding by ER chaperones.Biochimica et biophysica acta · 2013Review
- Quality control of integral membrane proteins by assembly-dependent membrane integration.Molecular cell · 2013Article
- A ubiquitin-like domain recruits an oligomeric chaperone to a retrotranslocation complex in endoplasmic reticulum-associated degradation.The Journal of biological chemistry · 2013Article
- MHC class I antigen presentation of DRiP-derived peptides from a model antigen is not dependent on the AAA ATPase p97.PloS one · 2013Article
- The p97 ATPase associates with EEA1 to regulate the size of early endosomes.Cell research · 2012Article
- How (specific) would like your T-cells today? Generating T-cell therapeutic function through TCR-gene transfer.Frontiers in immunology · 2012Article
- TorsinA participates in endoplasmic reticulum-associated degradation.Nature communications · 2011Article
- A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation.Molecular cell · 2011Article
- Proteostasis regulation at the endoplasmic reticulum: a new perturbation site for targeted cancer therapy.Cell research · 2011Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Endoplasmic reticulum (ER)-associated degradation (ERAD) of unassembled T-cell receptor alpha-chain (TCRalpha) is reliant on the presence of two basic residues in the transmembrane (TM) segment of TCRalpha. The precise role of these residues in ER quality control is unclear. Here, we show that a TCRalpha mutant lacking these intramembrane charged residues has a tendency to form homooligomers through an interchain disulfide bond that involves a specific pair of cysteine residues. Covalent oligomerization of TCRalpha appears to stabilize it at the ER membrane. The presence of a single lysine residue at specific positions within the TCRalpha TM domain abolishes its oligomerization and causes its rapid degradation. Conversely, when TCRalpha oligomerization is induced by a bivalent compound, the degradation of TCRalpha is inhibited. Together, these results suggest that the intramembrane charged residues in TCRalpha do not function as a signal for substrate recognition in ERAD. Instead, their primary role is to reduce TCRalpha oligomerization, maintaining it in a retrotranslocation-competent state. Our results also suggest that the ERAD machinery is inefficient when coping with oligomerized substrates, indicating a requirement for chaperone-mediated protein disassembly in the ER lumen prior to retrotranslocation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.