Dataset Information

Identification of the protein interaction network of STAG2 protein isoforms with inclusion and exclusion of exon32

ABSTRACT: This study involves the identification of specific interactors for STAG2ex32+ and STAG2ex32delta. Plasmids expressing YFP-STAG2 isoforms were transfected into HCT116OsTIR cells using untransfected cells as mock control. 40h post transfection, whole cell lysates were extracted and STAG2 isoforms were immunoprecipiated using GFP-TRAP. An unspecific GFP-TRAP pulldown was also conducted using lysates from untransfected cells to assess for unspecific protein binding to the beads (Mock). Significant proteins were determined by label-free quantification and statistical analysis using MaxQuant and MSstats.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Colon Cancer

SUBMITTER: Silvia Surinova

LAB HEAD: Silvia Surinova

PROVIDER: PXD041975 | Pride | 2023-05-04

REPOSITORIES: Pride

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Publications

Cohesin-independent STAG proteins interact with RNA and R-loops and promote complex loading.

Porter Hayley H Li Yang Y Neguembor Maria Victoria MV Beltran Manuel M Varsally Wazeer W Martin Laura L Cornejo Manuel Tavares MT Pezić Dubravka D Bhamra Amandeep A Surinova Silvia S Jenner Richard G RG Cosma Maria Pia MP Hadjur Suzana S

eLife 20230403

Most studies of cohesin function consider the Stromalin Antigen (STAG/SA) proteins as core complex members given their ubiquitous interaction with the cohesin ring. Here, we provide functional data to support the notion that the SA subunit is not a mere passenger in this structure, but instead plays a key role in the localization of cohesin to diverse biological processes and promotes loading of the complex at these sites. We show that in cells acutely depleted for RAD21, SA proteins remain boun ...[more]

PMID: 37010886

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Project description:Background: Aldo-keto reductase (AKR) 1C family member 3 (AKR1C3), one of four identified human AKR enzymes, catalyzes steroid, prostaglandin, and xenobiotic metabolism. In the prostate, AKR1C3 is up-regulated in localized and advanced prostate adenocarcinoma, and is associated with prostate cancer (PCa) aggressiveness. Here we provide initial evidence for potential roles of AKR1C3 in PCa progression. Methods: Spatial distribution of AKR1C3 was analyzed using immunohistochemical staining in prostate adenocarcinoma tissue array. Human PCa PC-3 cells were stably transfected with AKR1C3 cDNA to establish PC3-AKR1C3 transfectants. Microarray and bioinformatics analyses were performed to identify pathways that are activated by elevated AKR1C3 expression in PCa cells. Functional confirmation of microarray and bioinformatics results was performed by immunoblot analysis and an in vitro Matrigel angiogenesis assay. Results: Elevated AKR1C3 expression was specifically limited to human prostate adenocarcinoma. Microarray and bioinformatics analysis suggested that elevated AKR1C3 expression in PC-3 cells modulates estradiol and androgen metabolism and activates insulin growth factor (IGF)-1 and Akt signaling pathways. Immunoblots confirmed that phosphorylated levels of IGF-1 receptor (IGF-1R) and Akt are significantly up-regulated in PC3-AKR1C3 as compared to mock transfectants. PC3-AKR1C3 transfectants promoted endothelial cell tube formation in Matrigel as compared to parental PC-3 cells and mock transfectants. Conclusion: Microarray and bioinformatics data followed by biological analyses suggest that elevated AKR1C3 expression in PC-3 cells promotes PCa angiogenesis and aggressiveness. These results suggest AKR1C3 can promote the aggressiveness of PCa through modulating estrogen and androgen metabolism with subsequent activation of growth factor IGF-1 and cytoplasmic Akt signaling pathways. Total RNA from mock- and ACR1C3 transfected PC-3 cells was isolated, with 2 or 3 biological replicates each. Gene expression data from AKR1C3 transfected PC-3 cells were compared with mock-transfected data.

Dataset Information

Identification of the protein interaction network of STAG2 protein isoforms with inclusion and exclusion of exon32

Publications

Cohesin-independent STAG proteins interact with RNA and R-loops and promote complex loading.

Similar Datasets

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