ArticleEMBO reports2016
UBQLN4 recognizes mislocalized transmembrane domain proteins and targets these to proteasomal degradation.
Article in EMBO reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 69 citations in OpenAlex.
- MicroRNA-181 influences Alzheimer's risk by regulating neprilysin and microtubule-associated tau pathways, offering a novel target.bioRxiv : the preprint server for biology · 2026Article
- A mitochondria-driven quality control mechanism for peroxisomal membrane proteins.Nature communications · 2026Article
- A conformation-dependent hydrophobic degron determines Rab9a-mediated vesicular trafficking.The Journal of biological chemistry · 2026Article
- UBQLN2 is necessary for UBE3A-mediated proteasomal degradation of the domesticated retroelement PEG10.Journal of cell science · 2025Article
- The degradation of extended protein isoforms points to a misfiring translation initiation process.Molecular genetics and genomics : MGG · 2025Article
- UBQLN2 in neurodegenerative disease: mechanistic insights and emerging therapeutic potential.Biochemical Society transactions · 2025Review
- TanGIBLE: A selective probe for evaluating hydrophobicity-exposed defective proteins in live cells.The Journal of cell biology · 2025Article
- The rapid degradation of translated upstream regions points to an inefficient translation initiation process.bioRxiv : the preprint server for biology · 2024Article
- Dipeptidyl peptidases and E3 ligases of N-degron pathways cooperate to regulate protein stability.The Journal of cell biology · 2024Article
- Chikungunya virus infection disrupts MHC-I antigen presentation via nonstructural protein 2.PLoS pathogens · 2024Article
- Chikungunya virus infection disrupts MHC-I antigen presentation via nonstructural protein 2.bioRxiv : the preprint server for biology · 2023Article
- Proteotoxic stresses stimulate dissociation of UBL4A from the tail-anchored protein recognition complex.The Biochemical journal · 2023Article
- Shared Pathogenicity Features and Sequences between EBV, SARS-CoV-2, and HLA Class I Molecule-binding Motifs with a Potential Role in Autoimmunity.Clinical reviews in allergy & immunology · 2023Review
- Ubiquitin-independent proteasomal degradation driven by C-degron pathways.Molecular cell · 2023Article
- Protein quality control machinery supports primary ciliogenesis by eliminating GDP-bound Rab8-family GTPases.iScience · 2023Article
- BAG6 supports stress fiber formation by preventing the ubiquitin-mediated degradation of RhoA.Molecular biology of the cell · 2023Article
- UBQLN2 restrains the domesticated retrotransposon PEG10 to maintain neuronal health in ALS.eLife · 2023Article
- Coronary artery disease-associated immune geneFrontiers in cardiovascular medicine · 2023Article
- CCDC134 facilitates T cell activation through the regulation of early T cell receptor signaling.Frontiers in immunology · 2023Article
- Conserved degronome features governing quality control associated proteolysis.Nature communications · 2022Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The majority of transmembrane proteins are integrated into the endoplasmic reticulum (ER) by virtue of a signal sequence-mediated co-translational process. However, a substantial portion of transmembrane proteins fails to reach the ER, leading to mislocalized cytosolic polypeptides. Their appropriate recognition and removal are of the utmost importance to avoid proteotoxic stress. Here, we identified UBQLN4 as a BAG6-binding factor that eliminates newly synthesized defective polypeptides. Using a truncated transmembrane domain protein whose degradation occurs during a pre-ER incorporation process as a model, we show that UBQLN4 recognizes misassembled proteins in the cytoplasm and targets these to the proteasome. We suggest that the exposed transmembrane segment of the defective polypeptides is essential for the UBQLN4-mediated substrate discrimination. Importantly, UBQLN4 recognizes not only the defective model substrate but also a pool of endogenous defective proteins that were induced by the depletion of the SRP54 subunit of the signal recognition particle. This study identifies a novel quality control mechanism for newly synthesized and defective transmembrane domain polypeptides that fail to reach their correct destination at the ER membrane.
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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.