GO:0061945 regulation of protein K48-linked ubiquitination: Mechanism, Genes, Functions and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0061945 describes any process that modulates the rate, frequency or extent of K48-linked ubiquitination, the ubiquitin chain type that typically targets substrate proteins for proteasomal degradation.
• K48-linked ubiquitination is controlled by the opposing activities of E3 ubiquitin ligases, which attach K48-linked chains, and deubiquitinases (DUBs), which remove them.
• E3 ligases such as TRIM31, Triad3A, NEDD4, SOCS2 and MARCH7 regulate K48-linked ubiquitination of substrates including LOX-1, TLR9, TAK1, SLC7A11 and MARCH7 itself [1,3,4,6,8].
• DUBs such as USP7 can reverse K48-linked ubiquitination and stabilize substrates such as KRAS, linking this process to cancer.
• Dysregulation of K48-linked ubiquitination contributes to cancer, diabetic cardiomyopathy, atherosclerosis, preeclampsia, glomerulonephritis and ferroptosis-related disease [1,2,3,4,6,8].
• CRISPR knockout, point-mutation, knock-in and overexpression models allow causal testing of E3 ligase, DUB and substrate genes in this pathway.
Description
GO:0061945, regulation of protein K48-linked ubiquitination, is a biological process that controls the addition or removal of K48-linked polyubiquitin chains on substrate proteins. K48-linked ubiquitination is a protein ubiquitination process in which a polymer of ubiquitin is formed through linkages between lysine residues at position 48 of the ubiquitin monomers, and this chain type targets the substrate protein for degradation. Because this modification is a central determinant of protein stability, its regulation shapes nearly every cellular decision, from immune signaling to cell death and metabolism [1,3,4,6,7,8].
regulation of protein K48-linked ubiquitination At A Glance
| GO ID | GO:0061945 |
|---|---|
| GO term | regulation of protein K48-linked ubiquitination |
| Ontology | biological_process |
| Synonym | none |
| Major function | Modulates the rate, frequency or extent of K48-linked ubiquitination, which targets substrate proteins for degradation |
| Chain linkage | Ubiquitin polymers formed through lysine 48 of ubiquitin monomers |
| Main enzymes | E3 ubiquitin ligases and deubiquitinases |
| Representative regulators | TRIM31, Triad3A, NEDD4, SOCS2, MARCH7, USP7, BAG2 |
| Disease relevance | Cancer, cardiomyopathy, atherosclerosis, preeclampsia, glomerulonephritis, ferroptosis-related disease |
What Is GO:0061945?
In simple terms, GO:0061945 is the set of processes that tune how much K48-linked ubiquitin is attached to a target protein. The QuickGO definition states that it is any process that modulates the rate, frequency or extent of protein K48-linked ubiquitination, a protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 48 of the ubiquitin monomers, is added to a protein. K48-linked ubiquitination targets the substrate protein for degradation. Regulation therefore includes the activity of E3 ubiquitin ligases that build K48 chains, deubiquitinases that disassemble them, and any upstream signaling that changes the efficiency of these enzymes [1,3,4,6,7,8].
Why Is regulation of protein K48-linked ubiquitination Important in Cell Biology?
Regulation of K48-linked ubiquitination is important because it sets the lifetime of key regulatory proteins and therefore controls signaling output, stress responses and cell fate. Experimental evidence shows that altering this process changes disease phenotypes: Triad3A-mediated K48-linked ubiquitination and degradation of TLR9 impairs mitochondrial bioenergetics and exacerbates diabetic cardiomyopathy, SOCS2-enhanced ubiquitination of SLC7A11 promotes ferroptosis and radiosensitization in hepatocellular carcinoma, and macrophage-specific TRIM31 reduces atherosclerotic plaque formation by targeting LOX-1. Conversely, deubiquitinases such as USP7 can remove K48-linked chains and stabilize substrates such as KRAS in non-small cell lung cancer. These findings make GO:0061945 a high-value target for mechanistic and therapeutic research.
• Controls proteasomal degradation of substrates, thereby determining protein half-life and signaling strength [1,3,4,6,7,8].
• Regulates immune and inflammatory signaling, for example through TLR9 degradation by Triad3A and STING stabilization by BAG2.
• Modulates cell death pathways, including ferroptosis via SLC7A11 and MARCH7 [1,4].
• Contributes to cardiovascular disease, including diabetic cardiomyopathy and atherosclerosis [3,6].
• Is implicated in cancer progression and therapy response, for example KRAS stabilization by USP7 and SLC7A11-driven radiosensitization [4,7].
• Participates in pregnancy-related pathology through NEDD4-mediated ubiquitination of TAK1 in preeclampsia.
• Provides druggable nodes because E3 ligases and DUBs are enzymes with defined catalytic pockets [1,3,4,6,7,8].
• Can be studied with CRISPR knockout, point-mutation, knock-in and overexpression models to establish causality.
What Happens During regulation of protein K48-linked ubiquitination?
Substrate recognition by E3 ubiquitin ligases
In simple terms: E3 ligases choose which proteins get tagged with K48-linked ubiquitin chains.
The first step in regulation of K48-linked ubiquitination is recognition of a substrate by an E3 ubiquitin ligase. For example, the E3 ligase Triad3A mediates K48-linked ubiquitination and degradation of TLR9, and this event impairs mitochondrial bioenergetics and exacerbates diabetic cardiomyopathy. Similarly, SOCS2 enhances ubiquitination of SLC7A11 and promotes ferroptosis and radiosensitization in hepatocellular carcinoma. Macrophage-specific TRIM31 targets LOX-1 for K48-linked ubiquitination and reduces atherosclerotic plaque formation. These examples show that substrate selection by E3 ligases is a decisive regulatory step in GO:0061945 [3,4,6].
Assembly of K48-linked ubiquitin chains
In simple terms: Ubiquitin molecules are linked together through lysine 48 to form a degradation signal.
Once a substrate is bound, the ubiquitination machinery builds a polyubiquitin chain through linkages between lysine residues at position 48 of the ubiquitin monomers. This K48-linked chain is the modification that targets the substrate protein for degradation. Experimental work on NEDD4-mediated ubiquitination of TAK1 in preeclampsia demonstrates that this chain type is functionally important in human pathology. The same principle applies to MARCH7, whose stabilization acts as a ferro-guardian against ferroptosis, indicating that K48-linked ubiquitination of MARCH7 itself is a regulated event.
Deubiquitination as a counter-regulatory step
In simple terms: Deubiquitinases can remove K48-linked chains and rescue the substrate from degradation.
Regulation of K48-linked ubiquitination is bidirectional. Deubiquitinases such as USP7 can deubiquitinate KRAS and promote non-small cell lung cancer, showing that removal of ubiquitin chains stabilizes substrates and can drive oncogenesis. BAG2 inhibits cervical cancer progression by modulating type I interferon signaling through stabilizing STING, a process that involves regulation of ubiquitin-dependent stability. Thus, the balance between E3 ligase and DUB activity determines the net level of K48-linked ubiquitination on a given substrate [5,7].
Proteasomal degradation and downstream consequences
In simple terms: K48-linked chains usually send the tagged protein to the proteasome for destruction.
The functional outcome of K48-linked ubiquitination is typically degradation of the substrate protein. This is illustrated by Triad3A-mediated degradation of TLR9, which impairs mitochondrial bioenergetics and exacerbates diabetic cardiomyopathy, and by SOCS2-enhanced ubiquitination of SLC7A11, which promotes ferroptosis and radiosensitization in hepatocellular carcinoma. In mesangial proliferative glomerulonephritis, Bruceine A protects nuclear receptor 4A1 from ubiquitin-degradation to alleviate disease, directly linking regulation of K48-linked ubiquitination to a human renal disorder. These studies show that the degradation step is where GO:0061945 exerts many of its biological effects [2,3,4].
Integration with cellular stress and metabolic signals
In simple terms: Stress and metabolic signals change how much K48-linked ubiquitination occurs.
Regulation of K48-linked ubiquitination is integrated with cellular stress responses. MARCH7 stabilization acts as a ferro-guardian against ferroptosis, connecting this process to oxidative stress and iron-dependent cell death. In diabetic cardiomyopathy, Triad3A-mediated K48-linked ubiquitination of TLR9 impairs mitochondrial bioenergetics, linking the pathway to metabolic stress. In preeclampsia, NEDD4-mediated ubiquitination of TAK1 regulates trophoblast necroptosis, showing that this process is embedded in stress-responsive signaling. Together, these findings indicate that GO:0061945 is a hub for stress and metabolic regulation [1,3,8].
Key Genes Involved in GO:0061945 regulation of protein K48-linked ubiquitination
The following genes and proteins are experimentally implicated in regulation of protein K48-linked ubiquitination (GO:0061945) according to the verified literature.
| Gene | Major Role | Research Relevance |
|---|---|---|
| TRIM31 | E3 ubiquitin ligase targeting LOX-1 for K48-linked ubiquitination | Macrophage-specific TRIM31 reduces atherosclerotic plaque formation |
| Triad3A | E3 ubiquitin ligase mediating K48-linked ubiquitination and degradation of TLR9 | Exacerbates diabetic cardiomyopathy by impairing mitochondrial bioenergetics |
| NEDD4 | E3 ubiquitin ligase mediating ubiquitination of TAK1 | Regulates trophoblast necroptosis in preeclampsia |
| SOCS2 | Enhances ubiquitination of SLC7A11 | Promotes ferroptosis and radiosensitization in hepatocellular carcinoma |
| MARCH7 | E3 ligase stabilized as a ferro-guardian against ferroptosis | Stabilizing MARCH7 protects against ferroptosis |
| USP7 | Deubiquitinase that deubiquitinates KRAS | Promotes non-small cell lung cancer |
| BAG2 | Modulates type I interferon signaling through stabilizing STING | Inhibits cervical cancer progression |
| NR4A1 | Nuclear receptor protected from ubiquitin-degradation by Bruceine A | Alleviates mesangial proliferative glomerulonephritis |
| TLR9 | Substrate of Triad3A-mediated K48-linked ubiquitination | Links ubiquitination to mitochondrial bioenergetics in diabetic cardiomyopathy |
| SLC7A11 | Substrate of SOCS2-enhanced ubiquitination | Controls ferroptosis and radiosensitization in hepatocellular carcinoma |
| LOX-1 | Substrate of TRIM31-mediated K48-linked ubiquitination | Reduces atherosclerotic plaque formation |
| KRAS | Substrate of USP7 deubiquitination | Promotes non-small cell lung cancer |
| STING | Stabilized by BAG2, affecting type I interferon signaling | Inhibits cervical cancer progression |
| TAK1 | Substrate of NEDD4-mediated ubiquitination | Regulates trophoblast necroptosis in preeclampsia |
| MARCH7 | E3 ligase whose stabilization protects against ferroptosis | Ferroptosis-related disease |
| NR4A1 | Protected from ubiquitin-degradation | Mesangial proliferative glomerulonephritis |
| TLR9 | K48-linked ubiquitination substrate | Diabetic cardiomyopathy |
How Is regulation of protein K48-linked ubiquitination Regulated?
Regulation of K48-linked ubiquitination is itself regulated by the opposing activities of E3 ligases and deubiquitinases, and by upstream signals that modify their recruitment or activity. For example, Triad3A-mediated K48-linked ubiquitination of TLR9 is a regulated event that impairs mitochondrial bioenergetics and exacerbates diabetic cardiomyopathy. SOCS2 enhances ubiquitination of SLC7A11, promoting ferroptosis and radiosensitization in hepatocellular carcinoma. Macrophage-specific TRIM31 targets LOX-1 for K48-linked ubiquitination and reduces atherosclerotic plaque formation. Conversely, USP7 deubiquitinates KRAS and promotes non-small cell lung cancer, showing that DUB activity can counteract K48-linked ubiquitination. BAG2 stabilizes STING and modulates type I interferon signaling, further illustrating that this process is controlled at the level of substrate stability. NEDD4-mediated ubiquitination of TAK1 in preeclampsia demonstrates that tissue-specific contexts also shape regulation.
regulation of protein K48-linked ubiquitination and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| TRIM31 | Atherosclerosis | Macrophage-specific knockout or overexpression in mouse models |
| Triad3A | Diabetic cardiomyopathy | Cardiomyocyte-specific knockout or overexpression |
| SOCS2 | Hepatocellular carcinoma and radiosensitization | Knockout or overexpression in liver cancer cell lines and xenografts |
| USP7 | Non-small cell lung cancer | Knockout or catalytic-dead point mutation in lung cancer cells |
| NEDD4 | Preeclampsia | Trophoblast-specific knockout or knockdown models |
Cancer
Regulation of K48-linked ubiquitination is directly linked to cancer. SOCS2-enhanced ubiquitination of SLC7A11 promotes ferroptosis and radiosensitization in hepatocellular carcinoma, indicating that this process can be exploited to sensitize tumors to radiation. USP7 deubiquitinates KRAS and promotes non-small cell lung cancer, showing that removal of K48-linked chains can stabilize an oncoprotein. BAG2 inhibits cervical cancer progression by modulating type I interferon signaling through stabilizing STING, linking ubiquitin regulation to anti-tumor immunity. These studies identify E3 ligases and DUBs as candidate therapeutic targets in oncology [4,5,7].
Cardiovascular and metabolic disease
Triad3A-mediated K48-linked ubiquitination and degradation of TLR9 impairs mitochondrial bioenergetics and exacerbates diabetic cardiomyopathy. Macrophage-specific E3 ubiquitin ligase TRIM31 reduces atherosclerotic plaque formation by targeting LOX-1, demonstrating that K48-linked ubiquitination in macrophages is protective in atherosclerosis. These findings place GO:0061945 at the intersection of metabolic stress, mitochondrial function and cardiovascular pathology [3,6].
Renal and pregnancy-related disorders
Bruceine A protects nuclear receptor 4A1 from ubiquitin-degradation to alleviate mesangial proliferative glomerulonephritis, directly implicating regulation of K48-linked ubiquitination in renal disease. Thrombospondin-1 regulates trophoblast necroptosis via NEDD4-mediated ubiquitination of TAK1 in preeclampsia, linking this process to pregnancy complications. These studies show that modulating K48-linked ubiquitination can alter disease outcomes in kidney and placental pathology [2,8].
Ferroptosis and cell death
Stabilizing MARCH7 acts as a ferro-guardian against ferroptosis, indicating that regulation of K48-linked ubiquitination controls iron-dependent cell death. SOCS2-enhanced ubiquitination of SLC7A11 promotes ferroptosis and radiosensitization in hepatocellular carcinoma, further connecting this pathway to ferroptosis. Together, these findings suggest that K48-linked ubiquitination is a determinant of cell death modality in cancer and other diseases [1,4].
From regulation of protein K48-linked ubiquitination-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Is an E3 ligase required for K48-linked ubiquitination of a substrate? | CRISPR knockout of the E3 ligase gene followed by ubiquitination assays [3,4,6] |
| Does a specific lysine in the substrate accept K48-linked chains? | Point mutation of the acceptor lysine to arginine (K-to-R) [3,4,8] |
| Does a disease-associated mutation alter substrate stability? | Knock-in of the patient mutation and measurement of protein half-life [2,7] |
| Where does the E3 ligase interact with the substrate? | Tagged knock-in of the E3 ligase or substrate for imaging and co-immunoprecipitation [1,5] |
| Does overexpression of a DUB stabilize an oncoprotein? | Overexpression of USP7 or other DUBs in cancer cell lines |
| Can restoring K48-linked ubiquitination rescue a disease phenotype? | Knock-in of a degradation-resistant or degradation-prone substrate variant [1,4] |
How to Study the regulation of protein K48-linked ubiquitination Process
| Method | What It Measures | Typical Application |
|---|---|---|
| K48-linkage-specific immunoblot | Levels of K48-linked ubiquitin chains on a substrate | Confirming E3 ligase activity [3,4,6,8] |
| Cycloheximide chase | Protein half-life | Testing degradation downstream of ubiquitination [2,7] |
| Proteasome inhibitor treatment | Dependence on proteasomal degradation | Validating K48-linked ubiquitination function [2,3,4] |
| CRISPR knockout | Requirement of a gene for ubiquitination | Testing E3 ligase or DUB necessity [3,6] |
| Point mutation (K-to-R) | Specificity of ubiquitin linkage or acceptor site | Defining K48 linkage [4,8] |
| Knock-in tagging | Localization and interactions of the modified protein | Imaging and co-immunoprecipitation [1,5] |
| Overexpression | Gain-of-function effects on substrate stability | Testing DUB or E3 ligase sufficiency |
| Proteomics | Global changes in protein abundance | Identifying downstream effectors [1,4,5] |
Ubiquitination assays
Direct measurement of K48-linked ubiquitination is typically performed by immunoprecipitation of the substrate followed by immunoblotting with K48-linkage-specific antibodies. This approach has been used to show Triad3A-mediated K48-linked ubiquitination of TLR9, SOCS2-enhanced ubiquitination of SLC7A11, TRIM31-mediated ubiquitination of LOX-1, and NEDD4-mediated ubiquitination of TAK1. These assays are essential for confirming that a candidate regulator acts on the K48 linkage specifically [3,4,6,8].
Protein stability and degradation assays
Cycloheximide chase assays and proteasome inhibitor treatments are used to determine whether K48-linked ubiquitination leads to degradation. For example, Bruceine A protects nuclear receptor 4A1 from ubiquitin-degradation in mesangial proliferative glomerulonephritis, and USP7 deubiquitinates KRAS and promotes non-small cell lung cancer. These methods establish the functional consequence of the ubiquitination event [2,7].
Genetic perturbation with CRISPR
CRISPR knockout, point mutation, knock-in and overexpression are used to test causality. Knockout of an E3 ligase such as TRIM31 or Triad3A can reveal its requirement for substrate ubiquitination and disease phenotypes [3,6]. Point mutation of ubiquitin or substrate lysines can define the linkage type [4,8]. Knock-in of tagged alleles enables visualization of protein interactions [1,5]. Overexpression of DUBs such as USP7 can test stabilization of oncoproteins.
Omics and bioinformatics
Transcriptomic and proteomic profiling can identify global changes in protein stability after perturbation of K48-linked ubiquitination regulators. For example, studies on MARCH7 stabilization and ferroptosis, SOCS2 and SLC7A11, and BAG2 and STING used molecular profiling to link ubiquitination changes to downstream pathways. Bioinformatics analysis of ubiquitination sites and E3-substrate networks helps prioritize candidates for functional validation [1,4,5].
How CRISPR Can Be Used to Study GO:0061945 regulation of protein K48-linked ubiquitination
Knockout
CRISPR knockout of E3 ligases or DUBs is used to test whether they are required for K48-linked ubiquitination of a substrate. For example, knockout of TRIM31 would test its role in LOX-1 ubiquitination and atherosclerosis, and knockout of Triad3A would test its role in TLR9 degradation and diabetic cardiomyopathy. Knockout of SOCS2 would test its requirement for SLC7A11 ubiquitination and ferroptosis. These models provide loss-of-function evidence for GO:0061945 [3,4,6].
Point Mutation
Point mutation of ubiquitin lysine 48 to arginine prevents K48-linked chain formation and is a classic tool to test the linkage requirement. Point mutation of substrate lysine acceptors can identify the specific residue that is ubiquitinated. Such approaches have been used to study NEDD4-mediated ubiquitination of TAK1 and SOCS2-enhanced ubiquitination of SLC7A11. These experiments define the molecular grammar of GO:0061945 [4,8].
Knock-in
Knock-in of tagged or mutant alleles allows precise tracking of ubiquitination substrates and regulators in their native context. For example, knock-in of a tagged MARCH7 or STING allele could reveal its stabilization and interactions [1,5]. Knock-in of a degradation-resistant NR4A1 variant could test protection from ubiquitin-degradation in glomerulonephritis. These models are valuable for linking specific residues to disease phenotypes [1,2,5].
Overexpression
Overexpression of E3 ligases or DUBs is used to test sufficiency. Overexpression of USP7 stabilizes KRAS and promotes non-small cell lung cancer, while overexpression of BAG2 stabilizes STING and modulates type I interferon signaling. Overexpression of SOCS2 enhances SLC7A11 ubiquitination and ferroptosis. These gain-of-function models complement knockout studies and strengthen causal inference for GO:0061945 [4,5,7].
How EDITGENE Supports regulation of protein K48-linked ubiquitination Research
Researchers studying regulation of protein K48-linked ubiquitination-related genes often need to determine whether a candidate gene is causally involved in substrate degradation, disease progression or therapy response. EDITGENE provides CRISPR-based cell models and screening services to test these hypotheses with rigor.
Contact EDITGENE today to design your custom CRISPR model for regulation of protein K48-linked ubiquitination research.
Frequently Asked Questions About regulation of protein K48-linked ubiquitination
What is GO:0061945?
GO:0061945 is the Gene Ontology term for regulation of protein K48-linked ubiquitination, any process that modulates the rate, frequency or extent of K48-linked ubiquitination, which targets substrate proteins for degradation.
What is K48-linked ubiquitination?
K48-linked ubiquitination is a protein ubiquitination process in which a polymer of ubiquitin is formed through linkages between lysine residues at position 48 of the ubiquitin monomers, and this chain type targets the substrate protein for degradation.
What genes are involved in regulation of protein K48-linked ubiquitination?
Genes experimentally implicated include TRIM31, Triad3A, NEDD4, SOCS2, MARCH7, USP7 and BAG2, which regulate substrates such as LOX-1, TLR9, TAK1, SLC7A11, KRAS and STING [1,3,4,5,6,7,8].
How is K48-linked ubiquitination regulated?
It is regulated by the opposing activities of E3 ubiquitin ligases that attach K48-linked chains and deubiquitinases that remove them, as shown for Triad3A and TLR9, SOCS2 and SLC7A11, TRIM31 and LOX-1, and USP7 and KRAS.
Which diseases are linked to K48-linked ubiquitination?
It is linked to cancer, diabetic cardiomyopathy, atherosclerosis, preeclampsia, mesangial proliferative glomerulonephritis and ferroptosis-related disease [1,2,3,4,6,7,8].
What is the difference between K48 and K63 ubiquitination?
K48-linked chains typically target proteins for proteasomal degradation, whereas other linkages such as K63 are generally associated with non-degradative signaling; GO:0061945 specifically covers regulation of the K48 linkage.
How can I study regulation of K48-linked ubiquitination?
Common methods include K48-linkage-specific immunoblotting, cycloheximide chase, proteasome inhibitor treatment, CRISPR knockout, point mutation, knock-in tagging, overexpression and proteomics [1,2,3,4,5,6,7,8].
What CRISPR models are useful for K48-linked ubiquitination research?
Knockout of E3 ligases or DUBs, point mutation of ubiquitin or substrate lysines, knock-in of tagged or mutant alleles, and overexpression of DUBs or E3 ligases are all useful [1,3,4,5,6,7,8].
Is K48-linked ubiquitination reversible?
Yes, deubiquitinases such as USP7 can remove K48-linked chains and stabilize substrates, as shown for KRAS in non-small cell lung cancer.
Why is regulation of K48-linked ubiquitination important for drug discovery?
Because E3 ligases and DUBs are enzymes with defined catalytic activities, they are tractable targets for modulating substrate stability in cancer, cardiovascular disease and other conditions [1,3,4,6,7,8].
Conclusion
GO:0061945, regulation of protein K48-linked ubiquitination, is a central biological process that controls protein degradation and thereby shapes immune signaling, cell death, metabolism and disease. Experimental studies have identified key E3 ligases such as TRIM31, Triad3A, NEDD4, SOCS2 and MARCH7, and deubiquitinases such as USP7, that regulate substrates including LOX-1, TLR9, TAK1, SLC7A11, KRAS and STING [1,3,4,5,6,7,8]. These findings link the pathway to cancer, cardiovascular disease, renal disease, preeclampsia and ferroptosis [1,2,3,4,6,7,8].
References
- 1. Huang W et al.. 2026. Stabilizing MARCH7 as a ferro-guardian against ferroptosis.. Cell 189(12):3553-3570.e30 PMID: 42049018
- 2. Hu H et al.. 2025. Bruceine A protects nuclear receptor 4A1 from ubiquitin-degradation to alleviate mesangial proliferative glomerulonephritis.. Signal Transduct Target Ther 10(1):397 PMID: 41345104
- 3. Kong C et al.. 2024. Triad3A-Mediated K48-Linked ubiquitination and degradation of TLR9 impairs mitochondrial bioenergetics and exacerbates diabetic cardiomyopathy.. J Adv Res 61:65-81 PMID: 37625569
- 4. Chen Q et al.. 2023. SOCS2-enhanced ubiquitination of SLC7A11 promotes ferroptosis and radiosensitization in hepatocellular carcinoma.. Cell Death Differ 30(1):137-151 PMID: 35995846
- 5. Yao S et al.. 2025. BAG2 Inhibits Cervical Cancer Progression by Modulating Type I Interferon Signaling through Stabilizing STING.. Adv Sci (Weinh) 12(29):e70005 PMID: 40364789
- 6. Zhang J et al.. 2026. Macrophage-Specific E3 Ubiquitin Ligase TRIM31 Reduces Atherosclerotic Plaque Formation by Targeting LOX-1.. Circulation 153(8):576-596 PMID: 41410044
- 7. Huang B et al.. 2024. USP7 deubiquitinates KRAS and promotes non-small cell lung cancer.. Cell Rep 43(11):114917 PMID: 39499616
- 8. Hu H et al.. 2024. Thrombospondin-1 Regulates Trophoblast Necroptosis via NEDD4-Mediated Ubiquitination of TAK1 in Preeclampsia.. Adv Sci (Weinh) 11(21):e2309002 PMID: 38569496
