ArticleThe Journal of biological chemistry2008
The single subunit transmembrane E3 ligase gene related to anergy in lymphocytes (GRAIL) captures and then ubiquitinates transmembrane proteins across the cell membrane.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 71 citations in OpenAlex.
- Claudin-1 Interacts with CD81 and Promotes the Progression of Colorectal Cancer.Oncology research · 2026Article
- Regulatory roles of E3 ubiquitin ligase RNF128 in inflammatory diseases and tumors.Journal of Cancer · 2026Review
- E3 ubiquitin ligase RNF128 promotes Lys63-linked polyubiquitination on SRB1 in macrophages and aggravates atherosclerosis.Nature communications · 2025Article
- The association ofArchives animal breeding · 2025Article
- RNF149 negatively regulates LPS/TLR4 signal transduction by ubiquitination-mediated CD63 degradation.Heliyon · 2024Article
- Protein networking: nicotinic acetylcholine receptors and their protein-protein-associations.Molecular and cellular biochemistry · 2024Review
- RNF128 expression in lung adenocarcinoma is a favorable prognostic factor associated with decreased tumor-associated macrophages.Thoracic cancer · 2023Article
- Receptor control by membrane-tethered ubiquitin ligases in development and tissue homeostasis.Current topics in developmental biology · 2022Article
- Pax5 mediates the transcriptional activation of the CD81 gene.Scientific reports · 2021Article
- Tetraspanins as Potential Modulators of Glutamatergic Synaptic Function.Frontiers in molecular neuroscience · 2021Review
- RNF128 suppresses the malignancy of colorectal cancer cells via inhibition of Wnt/β-catenin signaling.American journal of translational research · 2021Article
- Tetraspanins in the regulation of mast cell function.Medical microbiology and immunology · 2020Review
- Protease associated domain of RNF43 is not necessary for the suppression of Wnt/β-catenin signaling in human cells.Cell communication and signaling : CCS · 2020Article
- Structure, dynamics and immunogenicity of a catalytically inactive CComputational and structural biotechnology journal · 2020Article
- Beyond the Cell Surface: Targeting Intracellular Negative Regulators to Enhance T cell Anti-Tumor Activity.International journal of molecular sciences · 2019Review
- Ubiquitin Ligase RNF138 Promotes Episodic Ataxia Type 2-Associated Aberrant Degradation of Human CaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Tetraspanins Function as Regulators of Cellular Signaling.Frontiers in cell and developmental biology · 2017Review
- E3 ubiquitin ligase RNF128 promotes innate antiviral immunity through K63-linked ubiquitination of TBK1.Nature immunology · 2016Article
- TM4SF3 and AR: A Nuclear Complex that Stabilizes Both Proteins.Molecular endocrinology (Baltimore, Md.) · 2016Article
- A family of tetraspans organizes cargo for sorting into multivesicular bodies.Developmental cell · 2015Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The ubiquitin E3 ligase gene related to anergy in lymphocytes (GRAIL) (Rnf128) is a type 1 transmembrane protein that induces T cell anergy through the ubiquitination activity of its cytosolic RING finger. GRAIL also contains an equally large luminal region consisting primarily of an uncharacterized protease-associated (PA) domain. Using two-hybrid technology to screen for proteins that bound the PA domain we identified CD151, a member of the tetraspanin family of membrane proteins. GRAIL bound to the luminal/extracellular portion of both CD151 and the related tetraspanin CD81 using its PA domain, which promoted ubiquitination of cytosolic lysine residues. GRAIL exhibited specificity for lysines only within the tetraspanin amino terminus even in the presence of other cytosolic lysine residues in the substrate. GRAIL-mediated ubiquitination promoted proteasomal degradation and cell surface down-regulation of tetraspanins via Lys-48 linkages. As a result, the juxtaposition of PA and RING finger domains across a lipid bilayer facilitates the capture of transmembrane substrates for subsequent ubiquitination. These findings identify for the first time a single subunit E3 ligase containing a substrate-binding domain spatially restricted by a membrane from its E2 recruitment domain as well as an E3 ligase for members of the tetraspanin family.
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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.