ArticleJournal of cell science2014
BAG6 regulates the quality control of a polytopic ERAD substrate.
Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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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
27 citing papers in PubMed, 40 citations in OpenAlex.
- Ubiquitin and ubiquitin-like modifications in the endoplasmic reticulum stress response.The FEBS journal · 2026Review
- A conformation-dependent hydrophobic degron determines Rab9a-mediated vesicular trafficking.The Journal of biological chemistry · 2026Article
- The role of ER-associated degradation and ER-phagy in health and disease.Signal transduction and targeted therapy · 2026Review
- TanGIBLE: A selective probe for evaluating hydrophobicity-exposed defective proteins in live cells.The Journal of cell biology · 2025Article
- Interactome screening implicates BAG6 as a suppressor of UBQLN2 misfolding in ALS/FTD.Frontiers in molecular neuroscience · 2025Article
- E3 ubiquitin ligase rififylin has yin and yang effects on rabbit cardiac transient outward potassium currents (IThe Journal of biological chemistry · 2024Article
- Mechanisms of substrate processing during ER-associated protein degradation.Nature reviews. Molecular cell biology · 2023Review
- BAG6 supports stress fiber formation by preventing the ubiquitin-mediated degradation of RhoA.Molecular biology of the cell · 2023Article
- The Endoplasmic Reticulum and the Fidelity of Nascent Protein Localization.Cold Spring Harbor perspectives in biology · 2023Review
- CCDC134 facilitates T cell activation through the regulation of early T cell receptor signaling.Frontiers in immunology · 2023Article
- Article
- Mitochondrial antiviral-signalling protein is a client of the BAG6 protein quality control complex.Journal of cell science · 2022Article
- Order through destruction: how ER-associated protein degradation contributes to organelle homeostasis.The EMBO journal · 2022Review
- GET4 is a novel driver gene in colorectal cancer that regulates the localization of BAG6, a nucleocytoplasmic shuttling protein.Cancer science · 2022Article
- USP5 enhances SGTA mediated protein quality control.PloS one · 2022Article
- SGTA associates with intracellular aggregates in neurodegenerative diseases.Molecular brain · 2021Article
- HLA-B-associated transcript 3 (Bat3) stabilizes and activates p53 in a HAUSP-dependent manner.Journal of molecular cell biology · 2020Article
- The WRB Subunit of the Get3 Receptor is Required for the Correct Integration of its Partner CAML into the ER.Scientific reports · 2019Article
- BAG6 deficiency induces mis-distribution of mitochondrial clusters under depolarization.FEBS open bio · 2019Article
- The Ways of Tails: the GET Pathway and more.The protein journal · 2019Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
BAG6 participates in protein quality control and, here, we address its role in endoplasmic-reticulum-associated degradation (ERAD) by using the polytopic membrane protein OpD, an opsin degron mutant. Both BAG6 knockdown and BAG6 overexpression delay OpD degradation; however, our data suggest that these two perturbations are mechanistically distinct. Hence, BAG6 knockdown correlates with reduced OpD polyubiquitylation, whereas BAG6 overexpression increases the level of polyubiquitylated OpD. The UBL- and BAG-domains of exogenous BAG6 are dispensable for OpD stabilisation and enhanced levels of polyubiquitylated OpD. Thus, although endogenous BAG6 normally promotes OpD degradation, exogenous BAG6 expression delays this process. We speculate that overexpressed BAG6 subunits might associate with the endogenous BAG6 complex, resulting in a dominant-negative effect that inhibits its function. Interestingly, cellular levels of BAG6 also correlate with total steady-state polyubiquitylation, with Rpn10 (officially known as PSMD4) overexpression showing a similar effect. These findings suggest that perturbations of the levels of ubiquitin-binding proteins can impact upon cellular ubiquitin homeostasis. We propose that exogenous BAG6 perturbs the function of the BAG6 complex at a stage subsequent to substrate recognition and polyubiquitylation, most likely the BAG6-dependent delivery of OpD to the proteasome.
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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.