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ANXA10 Promotes Melanoma Metastasis by Suppressing the Ubiquitination of PKD1 Mediated by E3 Ligase TRIM41

ABSTRACT: ANXA10 Promotes Melanoma Metastasis by Suppressing the Ubiquitination of PKD1 Mediated by E3 Ligase TRIM41

PROVIDER: PRJNA731190 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR14595558_1.fastq.gz	Fastqsanger.gz
	SRR14595558_2.fastq.gz	Fastqsanger.gz
	SRR14595559_1.fastq.gz	Fastqsanger.gz
	SRR14595559_2.fastq.gz	Fastqsanger.gz
	SRR14595560_1.fastq.gz	Fastqsanger.gz

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ANXA10 Promotes Melanoma Metastasis by Suppressing the Ubiquitination of PKD1 Mediated by E3 Ligase TRIM41

Project description:Melanoma is a highly metastatic type of cancer which requires novel and effective targeted therapies. Annexin A10 (ANXA10), a member of annexin family, is a calcium and phospholipid binding protein. Considerable evidences indicate that ANXA10 is involved in tumor progression, but little is known about the involvement of ANXA10 in melanoma. In this study, we reported that ANXA10 expression was significantly up-regulated and correlated with melanoma progression. Knockout of ANXA10 profoundly reduced cell migration and metastatic activity of melanoma. Mechanistic investigations showed that ANXA10 knockout induced N- to E-cadherin switch by upregulating SMAD6, an inhibitory SMAD in TGF-β/ SMAD pathway. The negative regulation of ANXA10 on SMAD6 was dependent on PKD1. We demonstrated that ANXA10 interacted with PKD1 and inhibited E3 ligase TRIM41-mediated PKD1 degradation. In B16F10 melanoma cells, the protein levels of ANXA10 and PKD1 were negatively correlated with SMAD6, but positively related to cell migration. In addition, a negative correlation of ANXA10 and SMAD6 levels was also observed in clinical samples, which was associated with melanoma progression. Our findings suggest that ANXA10/PKD1/ SMAD6 axis might be new targets of therapeutic strategies for melanoma metastasis.

2021-05-20 | GSE174724 | GEO

BRCT phosphoprotein recognition, but not E3 ligase activity, is essential for BRCA1 tumor suppression

Project description:It has been recognized that BRCA1, in the form of the BRCA1/BARD1 heterodimer, acting as an ubiquitin E3 ligase offered a possible mechanism to explain its pleiotrophic nature of BRCA1 activity. Our observation that mice lacking BRCA1 enzymatic activity are viable apart from male sterility was unexpected. Our results suggest that the E3 ligase activity of BRCA1 is largely dispensable for normal development and is not essential for all BRCA1 functions. Thus, many of the known and unknown functions of BRCA1 are likely to be mediated independent of its ability to catalyze ubiquitination. The genome copy number patterns were studied on the mice tumors that lacks E3 ubiqitin ligase activity of BRCA1 and were compared to copy number profile of mice lacking p53 and both brca1 and p53. Array CGH was performed using Agilent mouse CGH microarray 244K kit. Genomic DNA isolated from tumor tissue and its corresponding mouse tail were labelled with two different dyes and hybridized simultaneously on to microarray slides to perform comparitive genomic hybridization.

2011-08-25 | E-GEOD-31673 | biostudies-arrayexpress

BRCT phosphoprotein recognition, but not E3 ligase activity, is essential for BRCA1 tumor suppression

2011-08-26 | GSE31673 | GEO

EGFR is a target of the tumor suppressor E3-ligase FBXW7

Project description:FBXW7 is and E3 ubiquitin ligase and is highly mutated in colorectal cancer. We used human colon organoids with engineered FBXW7 hotspot mutations to investigate novel targets of E3 ligase activity with a combined transcriptomic and proteomic approach uncovering the EGFR-MAPK pathway as highly regulated by the E3 ligase activity.

2024-04-03 | GSE246896 | GEO

The Hace1 E3 Ligase Modulates the Activity of Multiple Tumor Suppressive CRL E3 Ligases by binding to CAND1

Project description:The Hace1 E3 ligase is a tumor suppressor in stressed cells. Through unknown mechanisms, Hace1 indirectly targets the cyclin D1 proto-oncogene for proteasomal degradation during nutrient depletion. We now show that Hace1 targets HIF1alpha for VHL-dependent degradation during hypoxia. To better understand these diverse actions we performed mass spectrometry to identify Hace1-interacting proteins. We show that Hace1 interacts with cullin-associated NEDD8-dissociated protein 1 (CAND1) under nutrient depletion and hypoxia. CAND1 binds cullins and prevents their entry into cullin ring E3 ligase (CRL) complexes, thus blocking CRL activity. Hace1 binding releases CUL1/2 from CAND1, facilitating assembly of CRL complexes to degrade cyclin D1 and HIF1alpha, respectively. These findings suggest a broad role for Hace1 in regulating tumor suppressive CRL E3 ligases. In this study, we used gene expression profiling to characterize how Hace1 overexpression affect the transcriptional response to hypoxic stress Using Affymetrix exon-level microarrays, we compared the expression profile of HEK293 cells overexpressing either Hace1 or MSCV vector alone, under hypoxia or normoxia

2011-07-01 | E-GEOD-25452 | biostudies-arrayexpress

The E3 SUMO ligase Mms21 controls ribosome biogenesis

Project description:The budding yeast E3 SUMO ligase Mms21, a component of the Smc5-6 complex, regulates sister chromatid cohesion, DNA replication, and DNA repair. We identify a role for Mms21 in ribosome biogenesis. The mms21RINGD mutant exhibits reduced rRNA production, nuclear accumulation of 60S and 40S ribosomal proteins, and elevated Gcn4 translation. Genes involved in ribosome biogenesis and translation are down-regulated in the mms21RINGD mutant. Examining gene expression profile of mms21RINGD mutant compared to wild-type by RNA Seq using Ilumina sequencing

2015-06-13 | E-GEOD-69826 | biostudies-arrayexpress

E3 ligase TRIP12 affecting EZH2 ubiquitination in ENKTL

Project description:Effects of potential E3 ligase that mediates polyubiquitination of EZH2 in extranodal natural killer T cell lymphoma

2023-10-14 | PXD046145 |

A human multisubunit E3 ubiquitin ligase required for heterotrimeric G-protein Beta-subunit ubiquitination and cAMP signaling

Project description:Proteomics Data Associated with Young et al. "A human multisubunit E3 ubiquitin ligase required for heterotrimeric G-protein Beta-subunit ubiquitination and cAMP signaling"

2021-04-11 | MSV000087176 | MassIVE

The chromatin-binding protein PHF6 functions as an E3 ubiquitin ligase of H2BK120 via H2BK12Ac recognition for activation of trophectodermal genes

Project description:Epigenetic regulation is important for establishing lineage-specific gene expression during early development. Although signaling pathways have been well-studied for regulation of trophectoderm reprogramming, epigenetic regulation of trophectodermal genes with histone modification dynamics have been poorly understood. Here, we identify that plant homeodomain finger protein 6 (PHF6) is a key epigenetic regulator for activation of trophectodermal genes using RNA-sequencing and ChIP assays. PHF6 acts as an E3 ubiquitin ligase for ubiquitination of H2BK120 (H2BK120ub) via its extended plant homeodomain 1 (PHD1), while the extended PHD2 of PHF6 recognizes acetylation of H2BK12 (H2BK12Ac). Intriguingly, the recognition of H2BK12Ac by PHF6 is important for exerting its E3 ubiquitin ligase activity for H2BK120ub. Together, our data provide evidence that PHF6 is crucial for epigenetic regulation of trophectodermal gene expression by linking H2BK12Ac to H2BK120ub modification.

2020-07-13 | GSE144298 | GEO

An E3 ligase TRIM1 promotes colorectal cancer progression via K63-linked ubiquitination and activation of HIF1α

Project description:We determined the binding and ubiquitination of HIF1a by an E3 ligase TRIM1. IP experiments were performed from SW480 cells and Ms files were acquired on Q Exactive mass spectrometer. We analysed the differences of protein abundance, comparing the normalized intensity on distinct proteins from different groups.

2023-10-31 | PXD046557 |

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