GO:0070979 protein K11-linked ubiquitination: Mechanism, Genes, Functions and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0070979 (protein K11-linked ubiquitination) describes the assembly of ubiquitin polymers on substrate proteins through isopeptide bonds between lysine 11 (K11) of ubiquitin monomers, a modification that typically targets the substrate for proteasomal degradation.
• The anaphase-promoting complex/cyclosome (APC/C) is the canonical K11 chain-building machine, working together with the E2 enzyme UBE2S to elongate ubiquitin chains during mitosis.
• K11-linked ubiquitination is emerging as a central regulatory layer in cancer, immune signaling, ferroptosis, cuproptosis, and ER-associated degradation (ERAD) [1,2,6,7].
• TRIM-family E3 ligases such as TRIM3, TRIM21, and RNF115 catalyze K11-linked ubiquitination of specific substrates including SLC7A11, ID1, LPP, RAB1A, and RAB13 [1,2,4,6].
• Dysregulated K11-linked ubiquitination contributes to non-small cell lung cancer, esophageal squamous cell carcinoma, bladder cancer, triple-negative breast cancer, and septic acute lung injury [1,2,4,5,3].
• CRISPR knockout, point-mutation, knock-in, and overexpression models are essential tools for dissecting the causal role of K11-linked ubiquitination enzymes and substrates in disease [1,2,4].
Description
Protein K11-linked ubiquitination (GO:0070979) is a biological process in which ubiquitin monomers are first attached to a substrate protein and then extended into polyubiquitin chains through isopeptide linkages between lysine 11 residues of the ubiquitin monomers. Unlike K48-linked chains, which are the classic proteasomal targeting signal, K11-linked chains are assembled primarily by the anaphase-promoting complex/cyclosome (APC/C) together with the E2 conjugating enzyme UBE2S, and they also target substrate proteins for degradation. This process is therefore a key mechanism for controlling the abundance of mitotic regulators and many other short-lived proteins. Over the past decade, K11-linked ubiquitination has been implicated in a remarkably broad range of biological contexts, including cell-cycle progression, ER-associated degradation (ERAD), innate immune receptor trafficking, ferroptosis, cuproptosis, and tumor metastasis [1,2,4,6,7]. Specific E3 ligases such as TRIM3, TRIM21, and RNF115 have been shown to catalyze K11-linked ubiquitination of substrates including SLC7A11, ID1, LPP, RAB1A, and RAB13, thereby controlling cancer cell death, tumorigenesis, lymphatic metastasis, and TLR-mediated immune responses [1,2,4,6]. For researchers, GO:0070979 provides a precise ontological handle for annotating experiments that measure K11-specific ubiquitin chain formation, E3-E2-substrate relationships, and downstream degradation events. Because K11 linkages are structurally and functionally distinct from K48 and K63 linkages, accurate experimental models, including CRISPR-engineered cell lines, are required to assign causality to specific enzymes and substrates [1,2,4].
protein K11-linked ubiquitination At A Glance
| GO ID | GO:0070979 |
|---|---|
| GO term | protein K11-linked ubiquitination |
| Ontology | biological_process |
| Synonym | None listed in QuickGO |
| Major function | Assembly of K11-linked polyubiquitin chains that target substrate proteins for degradation |
| Canonical machinery | Anaphase-promoting complex/cyclosome (APC/C) with E2 enzyme UBE2S |
| Representative E3 ligases | TRIM3, TRIM21, RNF115 |
| Representative substrates | SLC7A11, ID1, LPP, RAB1A, RAB13 |
| Associated processes | Mitosis, ERAD, ferroptosis, cuproptosis, immune signaling, tumor metastasis |
What Is GO:0070979?
In our own words, GO:0070979 (protein K11-linked ubiquitination) is the post-translational process in which ubiquitin molecules are covalently attached to a target protein and then polymerized into chains via linkages between the lysine 11 residues of successive ubiquitin monomers. The resulting K11-linked polyubiquitin chains act as a degradation signal, and the anaphase-promoting complex is the best-characterized machinery that promotes degradation of mitotic regulators through this chain type.
Why Is protein K11-linked ubiquitination Important in Cell Biology?
Protein K11-linked ubiquitination is important because it is a major degradation signal that controls the lifetime of key regulatory proteins, and its dysregulation is directly linked to cancer progression, immune dysfunction, and cell-death pathways such as ferroptosis and cuproptosis [1,2,4,6,7]. Because K11 chains are built by a defined enzymatic cascade involving APC/C, UBE2S, and specific E3 ligases, this process offers tractable targets for experimental perturbation and therapeutic hypothesis testing [4,7].
• Controls degradation of mitotic regulators through APC/C-mediated K11 chain assembly.
• Drives ferroptosis in non-small cell lung cancer by promoting SLC7A11/xCT degradation via TRIM3.
• Suppresses esophageal squamous cell carcinoma tumorigenesis and promotes cuproptosis through TRIM21-mediated ID1 degradation.
• Promotes lymphatic metastasis of bladder cancer via UBE2S/TRIM21-dependent LPP ubiquitination.
• Regulates post-ER trafficking of TLRs and innate immune responses through RNF115-mediated RAB1A and RAB13 ubiquitination.
• Contributes to septic acute lung injury through macrophage TRIM21-dependent autophagy regulator ubiquitination.
• Participates in ER-associated degradation (ERAD) quality control.
• Is implicated in glucose metabolism reprogramming and immune evasion in triple-negative breast cancer.
• Provides a mechanistic explanation for how short-lived oncoproteins and tumor suppressors are turned over [1,2].
• Offers a defined enzymatic cascade (E1-E2-E3-substrate) for CRISPR-based causal studies [1,2,4].
What Happens During protein K11-linked ubiquitination?
Step 1: Activation and transfer of ubiquitin
In simple terms: Ubiquitin is first switched on by one enzyme and handed to a carrier enzyme.
In the canonical ubiquitination cascade, ubiquitin is activated by an E1 enzyme and transferred to an E2 conjugating enzyme; for K11 chain elongation, the E2 enzyme UBE2S is a key carrier that cooperates with the anaphase-promoting complex/cyclosome (APC/C) to build K11-linked chains. This step establishes the thioester-linked ubiquitin-E2 intermediate required for subsequent substrate modification.
Step 2: Substrate recognition by E3 ligases
In simple terms: A tagging machine chooses which protein will receive the ubiquitin chain.
E3 ligases provide substrate specificity. TRIM3 recognizes SLC7A11/xCT and promotes its K11-linked ubiquitination and degradation in non-small cell lung cancer. TRIM21 mediates K11-linked ubiquitination of ID1 in esophageal squamous cell carcinoma and of LPP in bladder cancer, where UBE2S interacts with TRIM21 to promote LPP ubiquitination [2,4]. RNF115 catalyzes K11-linked ubiquitination of RAB1A and RAB13 to regulate TLR trafficking.
Step 3: Assembly of K11-linked polyubiquitin chains
In simple terms: Ubiquitin units are linked together at a specific position to form a chain.
After the first ubiquitin is attached to the substrate, additional ubiquitin monomers are conjugated through isopeptide bonds between lysine 11 residues, generating K11-linked polyubiquitin chains. The anaphase-promoting complex promotes degradation of mitotic regulators by assembling these K11-linked chains, and UBE2S is the E2 that extends them.
Step 4: Substrate degradation and downstream outcomes
In simple terms: The tagged protein is destroyed, which changes what the cell does next.
K11-linked polyubiquitination targets the substrate protein for degradation. Degradation of SLC7A11 by TRIM3 facilitates ferroptosis in non-small cell lung cancer, degradation of ID1 by TRIM21 suppresses tumorigenesis and promotes cuproptosis in esophageal squamous cell carcinoma, and degradation of LPP downstream of UBE2S/TRIM21 promotes lymphatic metastasis of bladder cancer. In macrophages, TRIM21 knockout inhibits septic acute lung injury by downregulating autophagy regulator protein ubiquitination.
Step 5: Crosstalk with ERAD and immune trafficking
In simple terms: K11 chains also help the cell throw away misfolded proteins and control immune receptors.
K11-linked ubiquitination participates in ER-associated degradation (ERAD), a quality-control pathway that removes misfolded proteins from the endoplasmic reticulum. RNF115 inhibits post-ER trafficking of TLRs and TLR-mediated immune responses by catalyzing K11-linked ubiquitination of RAB1A and RAB13, showing that K11 chains regulate membrane trafficking in addition to degradation.
Key Genes Involved in GO:0070979 protein K11-linked ubiquitination
The following genes and proteins are experimentally validated components, writers, or substrates of K11-linked ubiquitination and are commonly studied in this pathway.
| Gene | Major Role | Research Relevance |
|---|---|---|
| UBE2S | E2 conjugating enzyme that extends K11-linked ubiquitin chains with APC/C | Central writer of K11 chains; interacts with TRIM21 to ubiquitinate LPP in bladder cancer |
| TRIM3 | E3 ligase that promotes K11-linked ubiquitination of SLC7A11/xCT | Drives ferroptosis in non-small cell lung cancer |
| TRIM21 | E3 ligase mediating K11-linked ubiquitination of ID1, LPP, and autophagy regulators | Suppresses tumorigenesis, promotes cuproptosis, and modulates septic acute lung injury [2,3,4] |
| RNF115 | E3 ligase catalyzing K11-linked ubiquitination of RAB1A and RAB13 | Regulates post-ER TLR trafficking and innate immune responses |
| SLC7A11 | Substrate of TRIM3-mediated K11-linked ubiquitination | Cystine/glutamate transporter whose degradation promotes ferroptosis |
| ID1 | Substrate of TRIM21-mediated K11-linked ubiquitination | Inhibitor of DNA binding protein whose degradation suppresses ESCC tumorigenesis |
| LPP | Substrate of UBE2S/TRIM21-mediated K11-linked ubiquitination | Lipoma preferred partner protein linked to bladder cancer lymphatic metastasis |
| RAB1A | Substrate of RNF115-mediated K11-linked ubiquitination | Small GTPase controlling ER-to-Golgi trafficking and TLR transport |
| RAB13 | Substrate of RNF115-mediated K11-linked ubiquitination | Small GTPase involved in membrane trafficking and immune receptor delivery |
| APC/C subunits | E3 ubiquitin ligase complex that assembles K11-linked chains on mitotic regulators | Canonical machinery for K11 chain formation and mitotic degradation [4,7] |
| HK1 | Hexokinase 1 stabilized in a K11-linked ubiquitination-related context | Linked to glucose metabolism reprogramming and immune evasion in triple-negative breast cancer |
| YTHDF1 | m6A reader whose stability is regulated by ubiquitination-related machinery | Controls cancer immune surveillance through mTORC1-mediated phosphorylation |
| USP5 | Deubiquitinase that stabilizes YTHDF1 | Counteracts ubiquitin-mediated degradation and modulates immune surveillance |
| circZNF148 | Circular RNA that drives glucose metabolism reprogramming via HK1 stabilization | Enhances metastasis and immune evasion in triple-negative breast cancer |
| Autophagy regulators | Substrates of TRIM21-mediated ubiquitination in macrophages | Modulate septic acute lung injury |
| TLRs | Immune receptors whose trafficking is controlled by K11-linked ubiquitination of RAB1A/RAB13 | Link K11 chains to innate immune signaling |
How Is protein K11-linked ubiquitination Regulated?
K11-linked ubiquitination is regulated at multiple levels. The anaphase-promoting complex/cyclosome provides cell-cycle timing and substrate specificity for K11 chain assembly, while the E2 enzyme UBE2S determines chain elongation. E3 ligases such as TRIM3, TRIM21, and RNF115 confer substrate selectivity and can be regulated by interacting partners, as shown by UBE2S interacting with TRIM21 to mediate LPP ubiquitination [1,2,4,6]. Deubiquitinases such as USP5 can counteract ubiquitin-mediated degradation and stabilize substrates like YTHDF1, adding a layer of reversibility. In addition, phosphorylation events, such as mTORC1-mediated phosphorylation, can influence the stability and function of ubiquitination-related proteins.
protein K11-linked ubiquitination and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| TRIM3 | Non-small cell lung cancer; ferroptosis | TRIM3 knockout and overexpression in NSCLC cell lines with SLC7A11 readouts |
| TRIM21 | Esophageal squamous cell carcinoma; cuproptosis; septic acute lung injury | TRIM21 knockout macrophages and ESCC cells with ID1 and autophagy markers [2,3] |
| UBE2S / TRIM21 | Bladder cancer lymphatic metastasis | UBE2S knockdown and TRIM21 knockout bladder cancer models with LPP ubiquitination assays |
| RNF115 | TLR trafficking and innate immune responses | RNF115 knockout immune cells with RAB1A/RAB13 ubiquitination and TLR trafficking assays |
| circZNF148 / HK1 | Triple-negative breast cancer metabolism and immune evasion | circZNF148 knockdown and HK1 overexpression in TNBC models |
K11-linked ubiquitination in lung cancer and ferroptosis
TRIM3 facilitates ferroptosis in non-small cell lung cancer by promoting K11-linked ubiquitination and degradation of SLC7A11/xCT. This links GO:0070979 directly to a regulated cell-death pathway and suggests that K11 chain writers can act as tumor-suppressive or tumor-promoting nodes depending on context.
K11-linked ubiquitination in esophageal and bladder cancer
TRIM21-mediated K11-linked ubiquitination of ID1 suppresses tumorigenesis and promotes cuproptosis in esophageal squamous cell carcinoma. In bladder cancer, UBE2S interacting with TRIM21 mediates K11-linked ubiquitination of LPP to promote lymphatic metastasis. Together these studies show that K11 chains can either restrain or drive tumor progression depending on the substrate and tissue context [2,4].
K11-linked ubiquitination in immune regulation and acute lung injury
RNF115 inhibits post-ER trafficking of TLRs and TLR-mediated immune responses by catalyzing K11-linked ubiquitination of RAB1A and RAB13. Macrophage TRIM21 knockout inhibits septic acute lung injury by downregulating autophagy regulator protein ubiquitination. These findings position K11-linked ubiquitination as a modulator of innate immunity and inflammatory injury [3,6].
K11-linked ubiquitination in breast cancer metabolism and immune evasion
circZNF148 drives glucose metabolism reprogramming to enhance metastasis and immune evasion via HK1 stabilization in triple-negative breast cancer. USP5 stabilizes YTHDF1 to control cancer immune surveillance through mTORC1-mediated phosphorylation. These studies connect ubiquitination-dependent stability control to metabolic and immune phenotypes in aggressive breast cancer [5,8].
From protein K11-linked ubiquitination-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Is TRIM3 required for SLC7A11 degradation and ferroptosis? | TRIM3 knockout NSCLC cell line with SLC7A11 K11-ubiquitination and ferroptosis assays |
| Does TRIM21-mediated ID1 ubiquitination suppress ESCC tumorigenesis? | TRIM21 knockout and ID1 knock-in ESCC models with cuproptosis readouts |
| Does UBE2S/TRIM21-driven LPP ubiquitination promote bladder cancer metastasis? | UBE2S knockdown and TRIM21 knockout bladder cancer cells in lymphatic metastasis models |
| How does RNF115 control TLR trafficking via RAB1A/RAB13? | RNF115 knockout immune cells with tagged RAB1A/RAB13 knock-in and trafficking imaging |
| Does macrophage TRIM21 modulate septic acute lung injury? | Macrophage-specific TRIM21 knockout mouse models with autophagy regulator ubiquitination readouts |
| Does HK1 stabilization drive TNBC metabolism and immune evasion? | HK1 overexpression and circZNF148 knockdown TNBC models with metabolic and immune assays |
How to Study the protein K11-linked ubiquitination Process
| Method | What It Measures | Typical Application |
|---|---|---|
| K11 linkage-specific immunoblot | Presence of K11-linked ubiquitin chains | Confirming E3 ligase activity on a substrate [1,2,4] |
| Mass spectrometry diGly enrichment | Ubiquitination sites and chain topology | Mapping K11 linkages on substrates |
| Co-immunoprecipitation | E3-E2-substrate interactions | Validating UBE2S-TRIM21-LPP complexes |
| Ferroptosis assays | Lipid peroxidation and cell death | Testing TRIM3-SLC7A11 axis in NSCLC |
| Cuproptosis assays | Copper-induced cell death markers | Testing TRIM21-ID1 axis in ESCC |
| Autophagy flux assays | Autophagic degradation activity | Testing TRIM21 knockout in septic acute lung injury |
| TLR trafficking imaging | Subcellular localization of TLRs | Testing RNF115-RAB1A/RAB13 axis |
| Metabolic flux assays | Glucose metabolism reprogramming | Testing circZNF148-HK1 axis in TNBC |
Ubiquitin chain linkage-specific assays
K11-linked ubiquitination can be detected using linkage-specific antibodies or mass spectrometry-based diGly enrichment, which distinguish K11 chains from K48 or K63 chains. These assays are essential to confirm that a given E3 ligase produces K11 linkages on a specific substrate [1,2,4].
Proteomics and interactomics
Affinity purification of ubiquitinated proteins followed by mass spectrometry can identify substrates and chain topologies. Studies of TRIM3, TRIM21, and RNF115 used ubiquitination assays to define SLC7A11, ID1, LPP, RAB1A, and RAB13 as K11-linked substrates [1,2,4,6].
Functional cell-death and immune assays
Ferroptosis, cuproptosis, autophagy, and TLR trafficking readouts are used to connect K11-linked ubiquitination to downstream phenotypes [1,2,3,6]. These functional assays complement biochemical ubiquitination data and establish biological relevance [1,2,3,6].
CRISPR-based perturbation
CRISPR knockout, point-mutation, knock-in, and overexpression models allow causal testing of E3 ligases, E2 enzymes, and substrates in K11-linked ubiquitination pathways [1,2,4]. Such models are particularly valuable when distinguishing K11-specific effects from other ubiquitin linkages [1,2,4].
How CRISPR Can Be Used to Study GO:0070979 protein K11-linked ubiquitination
Knockout
CRISPR knockout of E3 ligases such as TRIM3, TRIM21, or RNF115 can abolish K11-linked ubiquitination of their substrates and reveal downstream phenotypes, including ferroptosis resistance, altered tumorigenesis, or impaired TLR trafficking [1,2,3,6]. Macrophage TRIM21 knockout, for example, inhibits septic acute lung injury by downregulating autophagy regulator protein ubiquitination.
Point Mutation
Point mutations can be introduced into ubiquitin itself (for example, K11R) or into substrate lysine acceptor sites to test whether K11-linked chain formation is required for degradation and downstream biology [1,2,4]. Such mutants help distinguish K11-specific effects from other linkage types [1,2,4].
Knock-in
Tagged knock-in of substrates such as SLC7A11, ID1, LPP, RAB1A, or RAB13 enables endogenous-level tracking of K11-linked ubiquitination and degradation in physiologically relevant settings [1,2,4,6]. Knock-in of disease-associated variants can also test whether specific mutations alter K11 chain recognition [1,2].
Overexpression
Overexpression of E3 ligases, E2 enzymes, or substrates is widely used to amplify K11-linked ubiquitination signals and to test sufficiency in driving phenotypes such as ferroptosis, cuproptosis, or metastasis [1,2,4,5]. Overexpression of HK1, for instance, supports glucose metabolism reprogramming and immune evasion in triple-negative breast cancer.
How EDITGENE Supports protein K11-linked ubiquitination Research
Researchers studying protein K11-linked ubiquitination-related genes often need to determine whether a candidate gene is causally involved in substrate degradation, cell-death pathways, or tumor phenotypes. EDITGENE provides CRISPR-engineered cell models and screening services that allow precise interrogation of E3 ligases, E2 enzymes, and substrates in the K11-linked ubiquitination cascade.
Contact EDITGENE today to design your custom CRISPR model for protein K11-linked ubiquitination research.
Frequently Asked Questions About protein K11-linked ubiquitination
What is protein K11-linked ubiquitination?
Protein K11-linked ubiquitination (GO:0070979) is a process in which ubiquitin monomers are attached to a protein and then polymerized into chains through linkages between lysine 11 residues of ubiquitin, typically targeting the substrate for degradation.
What genes are involved in protein K11-linked ubiquitination?
Key genes include UBE2S, TRIM3, TRIM21, RNF115, and substrates such as SLC7A11, ID1, LPP, RAB1A, and RAB13 [1,2,4,6].
Which enzyme builds K11-linked ubiquitin chains?
The E2 enzyme UBE2S, working with the anaphase-promoting complex/cyclosome (APC/C), is a major builder of K11-linked ubiquitin chains.
How is K11-linked ubiquitination different from K48-linked ubiquitination?
Both can target proteins for degradation, but K11 chains are assembled through lysine 11 linkages and are canonically built by APC/C and UBE2S, whereas K48 chains are the classic proteasomal signal [4,7].
What diseases are linked to K11-linked ubiquitination?
It has been linked to non-small cell lung cancer, esophageal squamous cell carcinoma, bladder cancer, triple-negative breast cancer, septic acute lung injury, and immune regulation [1,2,3,4,5,6].
How does TRIM21 mediate K11-linked ubiquitination?
TRIM21 acts as an E3 ligase that promotes K11-linked ubiquitination of substrates such as ID1 and LPP, and it can cooperate with UBE2S in bladder cancer [2,4].
What is the role of RNF115 in K11-linked ubiquitination?
RNF115 catalyzes K11-linked ubiquitination of RAB1A and RAB13, thereby inhibiting post-ER trafficking of TLRs and TLR-mediated immune responses.
Can CRISPR be used to study K11-linked ubiquitination?
Yes, CRISPR knockout, point-mutation, knock-in, and overexpression models are widely used to test the causal roles of E3 ligases, E2 enzymes, and substrates in K11-linked ubiquitination [1,2,4].
What experimental methods detect K11-linked ubiquitination?
Linkage-specific antibodies, mass spectrometry-based diGly enrichment, co-immunoprecipitation, and functional cell-death or immune assays are commonly used [1,2,4,6,7].
Why is K11-linked ubiquitination important in cancer?
It controls the degradation of proteins that regulate ferroptosis, cuproptosis, metastasis, and immune evasion, making it a key mechanism in multiple cancer types [1,2,4,5].
Conclusion
Protein K11-linked ubiquitination (GO:0070979) is a distinct and biologically important ubiquitin chain type that targets substrates for degradation and is assembled by APC/C, UBE2S, and specific E3 ligases such as TRIM3, TRIM21, and RNF115 [1,2,4,6,7]. Its roles in ferroptosis, cuproptosis, tumor metastasis, immune trafficking, and acute lung injury make it a high-value area for mechanistic and translational research [1,2,3,4,5,6]. CRISPR-engineered cell models, combined with linkage-specific ubiquitination assays and functional readouts, provide a rigorous path to assign causality to K11-linked ubiquitination components [1,2,4]. EDITGENE supports this workflow with knockout, point-mutation, knock-in, overexpression, library screening, and bioinformatics services tailored to K11-linked ubiquitination research.
References
- 1. Wang Z et al.. 2024. TRIM3 facilitates ferroptosis in non-small cell lung cancer through promoting SLC7A11/xCT K11-linked ubiquitination and degradation.. Cell Death Differ 31(1):53-64 PMID: 37978273
- 2. Li L et al.. 2025. TRIM21-Mediated K11-Linked Ubiquitination of ID1 Suppresses Tumorigenesis and Promotes Cuproptosis in Esophageal Squamous Cell Carcinoma.. Adv Sci (Weinh) 12(35):e02501 PMID: 40652518
- 3. Xie F et al.. 2025. Macrophage TRIM21 knockout inhibits septic acute lung injury by downregulating autophagy regulator protein ubiquitination.. Autophagy 21(12):2650-2669 PMID: 40509575
- 4. Xiao K et al.. 2023. UBE2S interacting with TRIM21 mediates the K11-linked ubiquitination of LPP to promote the lymphatic metastasis of bladder cancer.. Cell Death Dis 14(7):408 PMID: 37422473
- 5. Jin Y et al.. 2026. circZNF148 Drives Glucose Metabolism Reprogramming to Enhance Metastasis and Immune Evasion via HK1 Stabilization in Triple-Negative Breast Cancer.. Adv Sci (Weinh) PMID: 42565531
- 6. Zhang ZD et al.. 2022. RNF115 Inhibits the Post-ER Trafficking of TLRs and TLRs-Mediated Immune Responses by Catalyzing K11-Linked Ubiquitination of RAB1A and RAB13.. Adv Sci (Weinh) 9(16):e2105391 PMID: 35343654
- 7. Lopata A et al.. 2020. Ubiquitination in the ERAD Process.. Int J Mol Sci 21(15) PMID: 32731622
- 8. Shao N et al.. 2025. USP5 stabilizes YTHDF1 to control cancer immune surveillance through mTORC1-mediated phosphorylation.. Nat Commun 16(1):1313 PMID: 39900921
