Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The Mechanism of NEDD8 Activation of CUL5 Ubiquitin E3 Ligases

ABSTRACT: HDX-MS analysis of the Neddylated ASB9 Cullin 5 E3 ligase complex with ARIH2

INSTRUMENT(S): Synapt G2-S HDMS, Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Elizabeth Komives

PROVIDER: MSV000084812 | MassIVE | Thu Jan 16 09:39:00 GMT 2020

SECONDARY ACCESSION(S): PXD017156

REPOSITORIES: MassIVE

ACCESS DATA

Json Xml

Similar Datasets

The Mechanism of NEDD8 Activation of CUL5 Ubiquitin E3 Ligases.

Project description: Not available

| S-EPMC7950132 | biostudies-literature

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

2011-07-01 | GSE25452 | GEO

CUL5-ARIH2 E3-E3 ubiquitin ligase structure reveals cullin-specific NEDD8 activation.

Project description: Not available

| S-EPMC8460447 | biostudies-literature

Elucidation of E3 Ubiquitin Ligase Specificity Through Proteome-wide Internal Degron Mapping

Project description:The ubiquitin-proteasome system plays critical roles in biology by regulating protein degradation. Despite their importance, precise recognition specificity is known for few of the 600 E3s. Here we establish a two-pronged strategy for identifying and mapping critical residues of internal degrons on a genome scale in HEK-293T cells. We employ Global Protein Stability profiling combined with machine learning to identify 15,800 peptides likely to contain sequence-dependent degrons. We combine this with scanning mutagenesis to define critical residues for over 5,000 predicted degrons. Focusing on Cullin-RING ligase degrons, we generated mutational fingerprints for 219 degrons and developed DegronID, a computational algorithm enabling the clustering of degron peptides with similar motifs. CRISPR analysis enabled the discovery of E3-degron pairs of which we uncover 16 pairs that revealed extensive degron variability and structural determinants. We provide the visualization of this data on the public DegronID Data Browser as a resource for future exploration.

2023-09-21 | GSE240610 | GEO

PRMT6 and PARP1 sequencing in non-treated MDA-MB-231 cells

Project description:Here, we examined the interactions between PRMT6, poly(ADP-ribose) polymerase 1 (PARP1), and the cullin 4 B (CUL4B)-Ring E3 ligase (CRL4B) complex, to form a transcription-repressive complex that co-occupies the core clock gene PER3 promoter.

2023-05-24 | GSE210947 | GEO

The ZSWIM8 ubiquitin ligase mediates target-directed microRNA degradation [dataset3]

Project description:MicroRNAs (miRNAs) associate with Argonaute (AGO) proteins to direct widespread post-transcriptional gene repression. Although association with AGO typically protects miRNAs from nucleases, extensive pairing to some unusual target RNAs can trigger miRNA degradation. Here we found that this target-directed miRNA degradation (TDMD) required the ZSWIM8 Cullin-RING E3 ubiquitin ligase. This and other findings suggested and supported a mechanistic model of TDMD in which target-directed proteolysis of AGO by the ubiquitin–proteasome pathway exposes the miRNA for degradation. Moreover, loss-of-function studies indicated that the ZSWIM8 Cullin-RING ligase accelerates degradation of numerous miRNAs in cells of mammals, flies, and nematodes, thereby specifying the half-lives of most short-lived miRNAs. These results elucidate the mechanism of TDMD and expand the inferred role of TDMD in shaping miRNA levels in bilaterian animals.

2020-12-18 | GSE163388 | GEO

CUL4B ChIP-sequencing in non-treated MDA-MB-231 cells

Project description:Cullin 4B (CUL4B) is a scaffold protein of the CUL4B-Ring E3 ligase (CRL4B) complex. Here, we found that CRL4B interacted with transcriptional corepressor complexes. Our results supporting CUL4B as a potential target of cancer therapy.

2021-03-25 | GSE124611 | GEO

The ZSWIM8 ubiquitin ligase mediates target-directed microRNA degradation [dataset 2]

2020-12-18 | GSE163387 | GEO

The ZSWIM8 ubiquitin ligase mediates target-directed microRNA degradation [datatset 7]

2020-12-18 | GSE163392 | GEO