GO:2000060 positive regulation of ubiquitin-dependent protein catabolic process: Mechanism, Genes, Functions and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:2000060 describes any process that activates or increases the frequency, rate or extent of ubiquitin-dependent protein catabolic process, the major route for selective protein degradation in eukaryotes.
• The term is a biological_process child of positive regulation of protein catabolic process and is mechanistically executed by E1, E2 and E3 enzymes, deubiquitinases and proteasome adaptors.
• Positive regulation of ubiquitin-dependent protein catabolic process controls receptor trafficking, cell-cycle progression, senescence and metabolic stress responses.
• Dysregulation of this process contributes to cancer, cardiovascular disease, neurodegeneration and immune evasion.
• Key experimental models include CRISPR knockout, point-mutation, knock-in and overexpression cell lines, complemented by ubiquitin proteomics and live-cell imaging.
• EDITGENE provides end-to-end CRISPR services to dissect positive regulation of ubiquitin-dependent protein catabolic process in disease-relevant cell models.
Description
GO:2000060, positive regulation of ubiquitin-dependent protein catabolic process, is a Gene Ontology biological_process term that captures any activity which activates or increases the frequency, rate or extent of ubiquitin-dependent protein catabolism. In practical terms, it covers the regulatory inputs that switch on or accelerate the tagging of substrate proteins with ubiquitin chains and their subsequent delivery to the proteasome or lysosome. Because ubiquitin-dependent degradation is a central mechanism for controlling protein abundance, this term is essential for understanding how cells reset signaling networks after stimulation, remove damaged proteins and enforce cell-cycle checkpoints. Researchers study GO:2000060 because its effectors are frequently mutated or dysregulated in human disease. For example, ubiquitin-dependent regulation of G protein-coupled receptor trafficking and signaling determines whether receptors are recycled or degraded, directly influencing drug responses. In cancer, ACTN1 promotes head and neck squamous cell carcinoma tumorigenesis and cisplatin resistance by enhancing MYH9-dependent degradation of GSK-3beta and integrin beta1-mediated phosphorylation of FAK, illustrating how positive regulation of ubiquitin-dependent catabolism can be co-opted for tumor survival. Similarly, protein arginine methyltransferase 5-mediated arginine methylation stabilizes Kruppel-like factor 4 to accelerate neointimal formation, showing that stabilization and degradation arms of the ubiquitin system are tightly balanced in vascular disease. The term also intersects with senescence and immune surveillance. p16-dependent increase of PD-L1 stability regulates immunosurveillance of senescent cells, demonstrating that ubiquitin-dependent turnover of immune checkpoint proteins shapes tissue aging and cancer immunity. In the heart, G protein-coupled receptor kinase 3 exacerbates diabetic heart injuries through direct phosphorylation of cannabinoid receptor 2, a process coupled to ubiquitin-dependent receptor regulation. Finally, feedback regulation of ubiquitination and phase separation of HECT E3 ligases reveals how E3 enzymes self-limit their activity, a core feature of positive regulation of ubiquitin-dependent protein catabolic process. Together, these studies position GO:2000060 as a hub for therapeutic target discovery and CRISPR model development.
positive regulation of ubiquitin-dependent protein catabolic process At A Glance
| GO ID | GO:2000060 |
|---|---|
| GO term | positive regulation of ubiquitin-dependent protein catabolic process |
| Ontology | biological_process |
| Definition | Any process that activates or increases the frequency, rate or extent of ubiquitin-dependent protein catabolic process. |
| Synonym | positive regulation of protein degradation tagging activity; positive regulation of protein ubiquitination during ubiquitin-dependent protein breakdown; positive regulation of protein ubiquitination during ubiquitin-dependent protein catabolism; positive regulation of protein ubiquitination during ubiquitin-dependent protein degradation; positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; positive regulation of protein ubiquitinylation during ubiquitin-dependent protein catabolic process; positive regulation of protein ubiquitinylation during ubiquitin-dependent protein catabolism; positive regulation of protein ubiquitylation during ubiquitin-dependent protein catabolic process; positive regulation of protein ubiquitylation during ubiquitin-dependent protein catabolism |
| Major function | Activates or increases ubiquitin-dependent protein catabolism, including substrate ubiquitination and proteasomal or lysosomal degradation. |
| Parent term | positive regulation of protein catabolic process |
| Related process | ubiquitin-dependent protein catabolic process |
| Aspect | biological_process |
What Is GO:2000060?
According to the Gene Ontology, GO:2000060 positive regulation of ubiquitin-dependent protein catabolic process is defined as any process that activates or increases the frequency, rate or extent of ubiquitin-dependent protein catabolic process. It is a biological_process term that sits downstream of ubiquitin-dependent protein catabolic process and encompasses molecular events such as enhanced substrate recognition by E3 ligases, increased E2 conjugating enzyme activity, accelerated polyubiquitin chain elongation, and improved delivery of ubiquitinated substrates to the proteasome or lysosome. The term is synonymous with positive regulation of protein degradation tagging activity and positive regulation of protein ubiquitination during ubiquitin-dependent protein breakdown, catabolism or degradation.
Why Is positive regulation of ubiquitin-dependent protein catabolic process Important in Cell Biology?
GO:2000060 is important because ubiquitin-dependent protein catabolism is the principal selective degradation system in eukaryotic cells, and its positive regulation determines the lifetime of key regulatory proteins such as cell-cycle effectors, signaling receptors and immune checkpoint molecules. Altering the rate of this process changes cellular decisions ranging from proliferation and senescence to apoptosis and immune evasion. Consequently, the term provides a mechanistic framework for interpreting how mutations, post-translational modifications and pharmacological inputs reshape the proteome in health and disease.
• Controls the half-life of cell-cycle regulators such as Aurora A, influencing mitosis and meiosis.
• Determines whether G protein-coupled receptors are recycled or degraded, affecting drug responsiveness.
• Regulates immune checkpoint protein stability, including PD-L1 in senescent cells.
• Contributes to cancer progression and chemoresistance, as shown for ACTN1 in head and neck squamous cell carcinoma.
• Modulates vascular remodeling through stabilization of Kruppel-like factor 4.
• Is implicated in diabetic heart injury via G protein-coupled receptor kinase 3 and cannabinoid receptor 2.
• Shapes proteasome substrate selection in fission yeast and other model organisms.
• Is self-limited by feedback regulation and phase separation of HECT E3 ligases.
• Provides a target space for CRISPR knockout, point-mutation and knock-in screens.
• Enables development of small-molecule modulators of E3 ligases and deubiquitinases.
What Happens During positive regulation of ubiquitin-dependent protein catabolic process?
Substrate recognition and E3 ligase activation
In simple terms: The cell first decides which protein should be destroyed by switching on a tagging enzyme.
Positive regulation of ubiquitin-dependent protein catabolic process begins when upstream signals activate or recruit E3 ubiquitin ligases to specific substrates. For example, G protein-coupled receptor kinase 3 phosphorylates cannabinoid receptor 2, which can promote ubiquitin-dependent regulation of receptor trafficking and signaling. In cancer cells, ACTN1 enhances MYH9-dependent degradation of GSK-3beta, illustrating how an adaptor protein can direct E3 activity toward a selected target. Feedback regulation of ubiquitination and phase separation of HECT E3 ligases further shows that E3 activation is spatially organized and self-limiting.
Ubiquitin chain assembly and elongation
In simple terms: A chain of ubiquitin molecules is built on the target protein, acting like a destruction tag.
Once a substrate is engaged, E1 activating enzymes, E2 conjugating enzymes and E3 ligases cooperate to attach ubiquitin moieties and elongate polyubiquitin chains. The type and length of the chain determine whether the substrate is routed to the proteasome or to lysosomal degradation. Positive regulation of this step can occur through increased E2 activity, enhanced E3 processivity or inhibition of deubiquitinases that would otherwise trim the chain. The HECT E3 ligase study demonstrates that phase separation can concentrate ubiquitination machinery and modulate chain assembly.
Proteasomal or lysosomal delivery
In simple terms: The tagged protein is transported to the cell's recycling center for breakdown.
Polyubiquitinated substrates are recognized by shuttle factors and delivered to the 26S proteasome or to endosomal sorting complexes for lysosomal degradation. Positive regulation of ubiquitin-dependent protein catabolic process can accelerate this delivery by increasing the availability of ubiquitin receptors or by modifying the substrate's localization. In fission yeast, proteasome regulation of petite-negativity demonstrates that proteasome capacity influences the outcome of ubiquitin-dependent catabolism. Similarly, ubiquitin-dependent regulation of G protein-coupled receptor trafficking determines whether receptors are sorted to the degradative pathway.
Feedback control and termination
In simple terms: The tagging system has brakes so it does not destroy proteins indefinitely.
Positive regulation of ubiquitin-dependent protein catabolic process is balanced by negative feedback loops that prevent excessive degradation. HECT E3 ligases can self-ubiquitinate and undergo phase separation, which limits their activity and protects essential substrates. Deubiquitinases remove ubiquitin chains and rescue substrates from degradation. In senescence, p16-dependent increase of PD-L1 stability shows that stabilization mechanisms can counteract degradation to maintain immune checkpoint expression. These feedback layers ensure that positive regulation is transient and context-specific.
Integration with cellular stress and metabolic signals
In simple terms: Stress and metabolic cues can speed up or slow down protein destruction.
Cellular stresses such as oxidative stress, metabolic imbalance and inflammation modulate the rate of ubiquitin-dependent protein catabolism. In diabetic heart injury, G protein-coupled receptor kinase 3 exacerbates damage through phosphorylation of cannabinoid receptor 2, linking stress signaling to ubiquitin-dependent receptor regulation. In vascular cells, protein arginine methyltransferase 5-mediated arginine methylation stabilizes Kruppel-like factor 4, showing that methylation and ubiquitination pathways intersect to control protein stability. These examples illustrate how positive regulation of ubiquitin-dependent protein catabolic process integrates diverse signaling inputs.
Key Genes Involved in GO:2000060 positive regulation of ubiquitin-dependent protein catabolic process
The following genes and proteins are experimentally implicated in positive regulation of ubiquitin-dependent protein catabolic process or its substrate-specific branches.
| Gene | Major Role | Research Relevance |
|---|---|---|
| UBB | Ubiquitin precursor | Core building block for ubiquitin chains; target for knockout studies of degradation capacity. |
| UBC | Polyubiquitin precursor | Provides ubiquitin monomers for chain assembly; relevant to proteotoxic stress models. |
| UBA1 | E1 ubiquitin-activating enzyme | Initiates ubiquitin activation; essential for all downstream ubiquitination. |
| UBE2D1 | E2 ubiquitin-conjugating enzyme | Supports polyubiquitin chain elongation; candidate for point-mutation studies. |
| NEDD4 | HECT E3 ligase | Regulates receptor and ion channel degradation; subject to feedback and phase separation. |
| SMURF1 | HECT E3 ligase | Controls TGF-beta signaling components; relevant to cancer and fibrosis models. |
| MDM2 | RING E3 ligase | Targets p53 for degradation; central to cancer and senescence research. |
| SKP2 | F-box E3 ligase subunit | Degrades cell-cycle inhibitors; linked to proliferation and tumorigenesis. |
| FBXW7 | F-box E3 ligase subunit | Recognizes phosphorylated substrates; frequently mutated in cancer. |
| CUL1 | Cullin scaffold | Assembles SCF E3 complexes; knockout alters global ubiquitination. |
| RBX1 | RING finger protein | Activates cullin-RING ligases; essential for E3 catalysis. |
| PSMD1 | Proteasome regulatory subunit | Controls proteasome capacity; relevant to fission yeast petite-negativity. |
| USP7 | Deubiquitinase | Removes ubiquitin from substrates; counteracts positive regulation. |
| ACTN1 | Actin-binding adaptor | Enhances MYH9-dependent degradation of GSK-3beta in head and neck cancer. |
| MYH9 | Myosin heavy chain | Participates in degradation complex for GSK-3beta. |
| PRMT5 | Arginine methyltransferase | Stabilizes KLF4 via methylation, opposing ubiquitination. |
| GRK3 | G protein-coupled receptor kinase | Phosphorylates cannabinoid receptor 2 in diabetic heart injury. |
| CNR2 | Cannabinoid receptor 2 | Substrate for GRK3-dependent regulation in cardiac stress. |
How Is positive regulation of ubiquitin-dependent protein catabolic process Regulated?
Positive regulation of ubiquitin-dependent protein catabolic process is controlled at multiple levels. E3 ligases are regulated by phosphorylation, arginine methylation and phase separation, as shown for HECT E3 ligases and PRMT5-dependent KLF4 stabilization. Deubiquitinases provide a counteracting layer by removing ubiquitin chains. Proteasome abundance and activity also set the ceiling for degradation, as demonstrated by proteasome regulation of petite-negativity in fission yeast. In signaling contexts, G protein-coupled receptor kinases such as GRK3 phosphorylate receptors to promote their ubiquitin-dependent trafficking. Finally, senescence programs can stabilize substrates such as PD-L1 through p16-dependent mechanisms, effectively reducing net degradation.
positive regulation of ubiquitin-dependent protein catabolic process and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| ACTN1 | Head and neck squamous cell carcinoma, cisplatin resistance | CRISPR knockout in HNSCC cell lines followed by cisplatin sensitivity assay |
| GRK3 | Diabetic heart injury | Cardiomyocyte-specific knockout or point-mutation knock-in in mouse models |
| PRMT5 | Neointimal formation, vascular remodeling | Smooth muscle cell knockout and methylation-deficient knock-in |
| MDM2 | Cancer, p53 degradation, senescence | Overexpression and point-mutation models in cancer cell lines |
| PSMD1 | Proteasome capacity, petite-negativity | Knockout in fission yeast and proteasome activity assays |
Cancer and chemoresistance
Positive regulation of ubiquitin-dependent protein catabolic process is co-opted in cancer to eliminate tumor suppressors and stabilize oncoproteins. ACTN1 promotes head and neck squamous cell carcinoma tumorigenesis and cisplatin resistance by enhancing MYH9-dependent degradation of GSK-3beta and integrin beta1-mediated phosphorylation of FAK. MDM2-mediated degradation of p53 is a classic example of how increased ubiquitin-dependent catabolism drives tumorigenesis. Targeting E3 ligases or deubiquitinases that control these events is a major therapeutic strategy.
Cardiovascular and metabolic disease
In the heart, G protein-coupled receptor kinase 3 exacerbates diabetic heart injuries through direct phosphorylation of cannabinoid receptor 2, linking ubiquitin-dependent receptor regulation to metabolic cardiomyopathy. In vascular smooth muscle, protein arginine methyltransferase 5-mediated arginine methylation stabilizes Kruppel-like factor 4 to accelerate neointimal formation, showing that opposing stabilization and degradation signals shape vascular remodeling. These findings suggest that modulating positive regulation of ubiquitin-dependent protein catabolic process could alter disease progression.
Senescence and immune surveillance
p16-dependent increase of PD-L1 stability regulates immunosurveillance of senescent cells, demonstrating that ubiquitin-dependent turnover of immune checkpoint proteins controls how senescent cells evade or attract immune cells. This connects GO:2000060 to aging, cancer immunity and immunotherapy resistance. Understanding the balance between PD-L1 ubiquitination and stabilization may reveal new targets for senolytic or immunomodulatory therapies.
Neurodegeneration and proteostasis
Although direct neurodegeneration citations are limited in this set, the general principle that impaired ubiquitin-dependent protein catabolism leads to toxic protein accumulation is supported by the core machinery described in receptor trafficking and proteasome studies. Defects in E3 ligases, deubiquitinases or proteasome subunits can cause proteotoxic stress, a hallmark of neurodegenerative diseases. Model systems such as fission yeast provide tractable platforms to dissect these pathways.
From positive regulation of ubiquitin-dependent protein catabolic process-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Is a candidate E3 ligase required for substrate degradation? | CRISPR knockout cell line plus substrate stability assay |
| Does a specific phosphorylation site control E3 activity? | Point-mutation knock-in of phospho-dead or phospho-mimetic residues |
| Does a disease-associated mutation alter ubiquitination? | Knock-in of the patient mutation followed by ubiquitin proteomics |
| Where does the E3 ligase localize during substrate recognition? | Tagged knock-in with fluorescent or affinity tag |
| Does overexpression of a deubiquitinase stabilize a substrate? | Doxycycline-inducible overexpression cell line |
| Which genes modify positive regulation of ubiquitin-dependent catabolism? | Genome-wide CRISPR library screening with a degradation reporter |
How to Study the positive regulation of ubiquitin-dependent protein catabolic process Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Ubiquitin proteomics | Ubiquitinated peptide abundance | Identify substrates of E3 ligases under positive regulation |
| Live-cell imaging | Substrate half-life and localization | Validate degradation reporters in knockout or knock-in cells |
| CRISPR knockout screening | Gene requirement for degradation | Discover positive regulators of ubiquitin-dependent catabolism |
| In vitro ubiquitination assay | E3 ligase catalytic activity | Mechanistic studies of HECT and RING ligases |
| Proteasome activity assay | Proteolytic capacity | Assess proteasome contribution in fission yeast models |
| Co-immunoprecipitation | Protein-protein interactions | Map E3-substrate and adaptor complexes |
| Phospho-specific immunoblotting | Signaling-dependent modifications | Test GRK3-CNR2 phosphorylation in cardiac models |
| Methylation assays | Arginine methylation status | Study PRMT5-dependent KLF4 stabilization |
Ubiquitin proteomics and mass spectrometry
Mass spectrometry-based ubiquitin proteomics can quantify ubiquitinated peptides and identify substrates whose ubiquitination increases upon positive regulation of ubiquitin-dependent protein catabolic process. This approach is useful for mapping E3 ligase substrates and for validating CRISPR knockout or point-mutation models.
Live-cell imaging of degradation reporters
Fluorescent reporters fused to degrons or substrates allow real-time measurement of degradation rates. Tagged knock-in cell lines expressing fluorescently labeled substrates can reveal how positive regulation alters protein half-life and localization.
CRISPR screening and functional genomics
Genome-wide CRISPR knockout or activation screens with a degradation-dependent reporter can identify genes that positively regulate ubiquitin-dependent protein catabolic process. Hits can be validated with focused libraries targeting E3 ligases, deubiquitinases and proteasome subunits.
Biochemical assays for E3 ligase activity
In vitro ubiquitination assays using recombinant E1, E2, E3 and substrate measure the catalytic rate of ubiquitin chain assembly. These assays complement cell-based models and help distinguish direct effects from indirect regulation.
How CRISPR Can Be Used to Study GO:2000060 positive regulation of ubiquitin-dependent protein catabolic process
Knockout
CRISPR knockout of E3 ligases, deubiquitinases or proteasome subunits is used to test whether a gene is required for positive regulation of ubiquitin-dependent protein catabolic process. For example, knocking out ACTN1 in head and neck squamous cell carcinoma cells can reveal its role in MYH9-dependent GSK-3beta degradation and cisplatin resistance. Knockout of PSMD1 in fission yeast can probe proteasome contribution to petite-negativity.
Point Mutation
Point-mutation knock-in can dissect phosphorylation or methylation sites that control E3 ligase activity. For instance, mutating the GRK3 phosphorylation site on cannabinoid receptor 2 can test its role in diabetic heart injury. Similarly, phospho-dead or phospho-mimetic mutations in HECT E3 ligases can reveal feedback regulation mechanisms.
Knock-in
Tagged knock-in of substrates or E3 ligases with fluorescent or affinity tags enables real-time tracking of ubiquitination and degradation. Knock-in of disease-associated mutations can model how patient variants alter positive regulation of ubiquitin-dependent protein catabolic process. This approach is valuable for studying receptor trafficking and immune checkpoint stability.
Overexpression
Doxycycline-inducible overexpression of E3 ligases, deubiquitinases or substrates can amplify or suppress ubiquitin-dependent degradation. Overexpressing PRMT5, for example, can test whether increased arginine methylation stabilizes KLF4 and accelerates neointimal formation. Overexpression of MDM2 can drive p53 degradation in cancer models.
How EDITGENE Supports positive regulation of ubiquitin-dependent protein catabolic process Research
Researchers studying positive regulation of ubiquitin-dependent protein catabolic process-related genes often need to determine whether a candidate gene is causally involved in substrate degradation, receptor trafficking or disease phenotypes. EDITGENE provides publication-ready CRISPR cell models and screening services to answer these questions with rigor and reproducibility.
Contact EDITGENE today to design your custom CRISPR model for positive regulation of ubiquitin-dependent protein catabolic process research.
Frequently Asked Questions About positive regulation of ubiquitin-dependent protein catabolic process
What is GO:2000060 positive regulation of ubiquitin-dependent protein catabolic process?
GO:2000060 is a Gene Ontology biological_process term defined as any process that activates or increases the frequency, rate or extent of ubiquitin-dependent protein catabolic process.
What genes are involved in positive regulation of ubiquitin-dependent protein catabolic process?
Key genes include E1, E2 and E3 enzymes such as UBA1, UBE2D1, NEDD4, MDM2 and SKP2, deubiquitinases such as USP7, proteasome subunits such as PSMD1, and adaptors such as ACTN1 and PRMT5.
How is ubiquitin-dependent protein catabolism positively regulated?
It is positively regulated by E3 ligase activation, enhanced E2 activity, inhibition of deubiquitinases, phosphorylation of substrates and feedback control of HECT E3 ligases.
Why is positive regulation of ubiquitin-dependent protein catabolic process important in cancer?
It can degrade tumor suppressors such as p53 and promote chemoresistance, as shown by ACTN1-mediated GSK-3beta degradation in head and neck cancer.
What diseases are linked to GO:2000060?
Cancer, diabetic heart injury, vascular remodeling, senescence and immune evasion are linked to altered positive regulation of ubiquitin-dependent protein catabolic process.
How can CRISPR be used to study positive regulation of ubiquitin-dependent protein catabolic process?
CRISPR knockout, point-mutation, knock-in and overexpression models can test whether specific genes control substrate ubiquitination and degradation.
What methods measure ubiquitin-dependent protein degradation?
Ubiquitin proteomics, live-cell imaging of degradation reporters, in vitro ubiquitination assays and proteasome activity assays are commonly used.
What is the role of HECT E3 ligases in this process?
HECT E3 ligases catalyze ubiquitin chain assembly and are regulated by feedback ubiquitination and phase separation, which limits their activity.
How does GRK3 relate to ubiquitin-dependent protein catabolic process?
GRK3 phosphorylates cannabinoid receptor 2, which is linked to ubiquitin-dependent receptor regulation in diabetic heart injury.
What cell models are suitable for studying GO:2000060?
Knockout, point-mutation knock-in, tagged knock-in and inducible overexpression cell lines in cancer, cardiac, vascular and immune cell backgrounds are suitable.
Conclusion
GO:2000060 positive regulation of ubiquitin-dependent protein catabolic process is a central biological_process term that connects ubiquitin machinery to protein turnover, signaling and disease. Its effectors include E1, E2 and E3 enzymes, deubiquitinases and proteasome components, and its dysregulation contributes to cancer, cardiovascular disease, senescence and immune evasion. CRISPR-based models and multi-omics methods provide powerful tools to dissect this process and identify therapeutic targets.
References
- 1. Majewska J et al.. 2024. p16-dependent increase of PD-L1 stability regulates immunosurveillance of senescent cells.. Nat Cell Biol 26(8):1336-1345 PMID: 39103548
- 2. Gao P et al.. 2025. G Protein-Coupled Receptor Kinase 3 Exacerbates Diabetic Heart Injuries Through Direct Phosphorylation of Cannabinoid Receptor 2 in Humans and Mice.. Circulation 152(12):882-898 PMID: 40772312
- 3. Cui L et al.. 2023. ACTN1 promotes HNSCC tumorigenesis and cisplatin resistance by enhancing MYH9-dependent degradation of GSK-3β and integrin β1-mediated phosphorylation of FAK.. J Exp Clin Cancer Res 42(1):335 PMID: 38057867
- 4. Liu H et al.. 2023. Protein arginine methyltransferase 5-mediated arginine methylation stabilizes Kruppel-like factor 4 to accelerate neointimal formation.. Cardiovasc Res 119(11):2142-2156 PMID: 37201513
- 5. Marchese A et al.. 2013. Ubiquitin-dependent regulation of G protein-coupled receptor trafficking and signaling.. Cell Signal 25(3):707-16 PMID: 23201781
- 6. Amberg KL et al.. 2025. Proteasome regulation of petite-negativity in fission yeast.. BMC Biol 23(1):302 PMID: 41068765
- 7. Li J et al.. 2023. Feedback regulation of ubiquitination and phase separation of HECT E3 ligases.. Proc Natl Acad Sci U S A 120(33):e2302478120 PMID: 37549262
- 8. Crane R et al.. 2004. Aurora A, meiosis and mitosis.. Biol Cell 96(3):215-29 PMID: 15182704
