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PD-L1 ubiquitination by MIB2 enables its translocation to the plasma membrane for tumor immune evasion

ABSTRACT: PD-L1 ubiquitination by MIB2 enables its translocation to the plasma membrane for tumor immune evasion

PROVIDER: PRJNA906110 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR22430454.fastq.gz	Fastqsanger.gz
	SRR22430455.fastq.gz	Fastqsanger.gz
	SRR22430456.fastq.gz	Fastqsanger.gz

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Similar Datasets

PD-L1 ubiquitination by MIB2 enables its translocation to the plasma membrane for tumor immune evasion

Project description:Programmed death-ligand 1 (PD-L1), a critical immune checkpoint ligand, is a transmembrane protein synthesized in the endoplasmic reticulum of tumor cells and transported to the plasma membrane to interact with programmed death 1 (PD-1) expressed on T cell surface. This interaction delivers co-inhibitory signals to T cells, thereby suppressing their function and evading antitumor immunity. Most companion or complementary diagnostic devices for PD-L1 expression levels in tumor cells used in the clinic or clinical trials require membranous staining. However, the mechanism driving PD-L1 translocation to the plasma membrane after de novo synthesis is poorly understood. Herein, we showed that mind bomb homolog 2 (MIB2) is required for PD-L1 transportation from the trans-Golgi network (TGN) to the plasma membrane of cancer cells. MIB2 deficiency leaded to fewer PD-L1 proteins on the tumor cell surface and promotes antitumor immunity in mice.We performed a single-cell RNA sequencing (scRNA-seq) of B16-F10 tumors from C57BL/6 syngeneic mice. Knockdown of MIB2 resulted in an increase in the percentage of CD8+ CTLs (approximately 5-fold) and CD4+/CD8+ effector/activated T cells (approximately 2-fold), indicating that MIB2 downregulation enhanced the antitumor immune activity centered on CD8+ CTLs and changed their transcriptional profile. Our findings demonstrate that non-proteolytic ubiquitination of PD-L1 by MIB2 is required for its transportation to the plasma membrane and tumor cells' immune evasion.

2023-12-31 | GSE218906 | GEO

PD-L1 translocation to the plasma membrane enables tumor immune evasion through MIB2 ubiquitination.

Project description:Programmed death-ligand 1 (PD-L1), a critical immune checkpoint ligand, is a transmembrane protein synthesized in the endoplasmic reticulum of tumor cells and transported to the plasma membrane to interact with programmed death 1 (PD-1) expressed on T cell surface. This interaction delivers coinhibitory signals to T cells, thereby suppressing their function and allowing evasion of antitumor immunity. Most companion or complementary diagnostic devices for assessing PD-L1 expression levels in tumor cells used in the clinic or in clinical trials require membranous staining. However, the mechanism driving PD-L1 translocation to the plasma membrane after de novo synthesis is poorly understood. Herein, we showed that mind bomb homolog 2 (MIB2) is required for PD-L1 transportation from the trans-Golgi network (TGN) to the plasma membrane of cancer cells. MIB2 deficiency led to fewer PD-L1 proteins on the tumor cell surface and promoted antitumor immunity in mice. Mechanistically, MIB2 catalyzed nonproteolytic K63-linked ubiquitination of PD-L1, facilitating PD-L1 trafficking through Ras-associated binding 8-mediated (RAB8-mediated) exocytosis from the TGN to the plasma membrane, where it bound PD-1 extrinsically to prevent tumor cell killing by T cells. Our findings demonstrate that nonproteolytic ubiquitination of PD-L1 by MIB2 is required for its transportation to the plasma membrane and tumor cell immune evasion.

| S-EPMC9888393 | biostudies-literature

PHF8 enables immune evasion by silencing endogenous retroelements

Project description:PHF8 enables immune evasion by silencing endogenous retroelements

| PRJNA877236 | ENA

PHF8 enables immune evasion by silencing endogenous retroelements.

Project description:PHF8 enables immune evasion by silencing endogenous retroelements.

| PRJNA870723 | ENA

PHF8 enables immune evasion by silencing endogenous retroelements [CHIP-seq]

Project description:PHF8 enables immune evasion by silencing endogenous retroelements [CHIP-seq]

| PRJNA870727 | ENA

PHF8 enables immune evasion by silencing endogenous retroelements [ChIP-seq]

Project description:PHF8 enables immune evasion by silencing endogenous retroelements [ChIP-seq]

| PRJNA877239 | ENA

PHF8 enables immune evasion by silencing endogenous retroelements [RNA-Seq]

Project description:PHF8 enables immune evasion by silencing endogenous retroelements [RNA-Seq]

| PRJNA870462 | ENA

PHF8 enables immune evasion by silencing endogenous retroelements [ATAC-seq]

Project description:PHF8 enables immune evasion by silencing endogenous retroelements [ATAC-seq]

| PRJNA870726 | ENA

CDK5-dependent phosphorylation and nuclear translocation of TRIM59 promotes macroH2A1 ubiquitination and tumorigenicity

Project description:CDK5-dependent phosphorylation and nuclear translocation of TRIM59 promotes macroH2A1 ubiquitination and tumorigenicity

| PRJNA542104 | ENA

CDK5-dependent phosphorylation and nuclear translocation of TRIM59 promotes macroH2A1 ubiquitination and tumorigenicity

Project description:Despite the development of adjuvant therapies, glioblastoma (GBM) patients remain incurable and justify the urgent need of new therapies. CDK5 functions a critical role in GBM and is a potential target for GBM. However, the mechanism by which CDK5 promotes GBM tumorigenicity remains largely unknown. Here we identify TRIM59 as a substrate of CDK5. EGFR-activated CDK5 directly binds to and phosphorylates TRIM59, a ubiquitin ligase at serine 308, which recruits PIN1 for cis-trans isomerization of TRIM59, leading to TRIM59 binding to importin a5 and nuclear translocation. Nuclear TRIM59 induces ubiquitination and degradation of the tumor suppressive histone variant macroH2A1, leading to enhanced STAT3 signaling activation and tumorigenicity. These findings are confirmed by inhibition of CDK5-activated TRIM59 activity that results in suppression of intracranial tumor growth. Correlative expressions of the components of this pathway are clinically prognostic. Our findings suggest targeting CDK5/TRIM59 signaling axis as a putative strategy for treating GBM.

2019-08-11 | GSE130949 | GEO

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