ArticleMolecular biology of the cell2009
Physical and functional interaction of transmembrane thioredoxin-related protein with major histocompatibility complex class I heavy chain: redox-based protein quality control and its potential relevance to immune responses.
Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
- TMX5/TXNDC15, a natural trapping mutant of the PDI family is a client of the proteostatic factor ERp44.Life science alliance · 2024Article
- TMX1, a disulfide oxidoreductase, is necessary for T cell function through regulation of CD3ζ.bioRxiv : the preprint server for biology · 2024Article
- Recent advances in vascular thiol isomerases and redox systems in platelet function and thrombosis.Journal of thrombosis and haemostasis : JTH · 2024Review
- Protein disulfide isomerase family mediated redox regulation in cancer.Advances in cancer research · 2023Review
- Introducing Thioredoxin-Related Transmembrane Proteins: Emerging Roles of Human TMX and Clinical Implications.Antioxidants & redox signaling · 2022Review
- Vascular thiol isomerases in thrombosis: The yin and yang.Journal of thrombosis and haemostasis : JTH · 2020Review
- Thioredoxin-Related Transmembrane Proteins: TMX1 and Little Brothers TMX2, TMX3, TMX4 and TMX5.Cells · 2020Review
- TMX2 Is a Crucial Regulator of Cellular Redox State, and Its Dysfunction Causes Severe Brain Developmental Abnormalities.American journal of human genetics · 2019Article
- Thioredoxin-related transmembrane protein 2 (TMX2) regulates the Ran protein gradient and importin-β-dependent nuclear cargo transport.Scientific reports · 2019Article
- Methods to identify the substrates of thiol-disulfide oxidoreductases.Protein science : a publication of the Protein Society · 2019Review
- Transmembrane thioredoxin-related protein TMX1 is reversibly oxidized in response to protein accumulation in the endoplasmic reticulum.FEBS open bio · 2017Article
- TMX1 determines cancer cell metabolism as a thiol-based modulator of ER-mitochondria Ca2+ flux.The Journal of cell biology · 2016Article
- Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides.Molecular biology of the cell · 2015Article
- The protective role of the transmembrane thioredoxin-related protein TMX in inflammatory liver injury.Antioxidants & redox signaling · 2013Article
- Identification and immunological characterization of thioredoxin transmembrane-related protein from Clonorchis sinensis.Parasitology research · 2013Article
- Disulfide bond formation in the mammalian endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2012Review
- The human protein disulfide isomerase gene family.Human genomics · 2012Article
- Reductive activation of type 2 ribosome-inactivating proteins is promoted by transmembrane thioredoxin-related protein.The Journal of biological chemistry · 2012Article
- Palmitoylated TMX and calnexin target to the mitochondria-associated membrane.The EMBO journal · 2012Article
- Novel thioredoxin-related transmembrane protein TMX4 has reductase activity.The Journal of biological chemistry · 2010Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the endoplasmic reticulum (ER), a variety of oxidoreductases classified in the thioredoxin superfamily have been found to catalyze the formation and rearrangement of disulfide bonds. However, the precise function and specificity of the individual thioredoxin family proteins remain to be elucidated. Here, we characterize a transmembrane thioredoxin-related protein (TMX), a membrane-bound oxidoreductase in the ER. TMX exists in a predominantly reduced form and associates with the molecular chaperon calnexin, which can mediate substrate binding. To determine the target molecules for TMX, we apply a substrate-trapping approach based on the reaction mechanism of thiol-disulfide exchange, identifying major histocompatibility complex (MHC) class I heavy chain (HC) as a candidate substrate. Unlike the classical ER oxidoreductases such as protein disulfide isomerase and ERp57, TMX seems not to be essential for normal assembly of MHC class I molecules. However, we show that TMX-class I HC interaction is enhanced during tunicamycin-induced ER stress, and TMX prevents the ER-to-cytosol retrotranslocation of misfolded class I HC targeted for proteasomal degradation. These results suggest a specific role for TMX and its mechanism of action in redox-based ER quality control.
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