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BACE2 and lipid metabolism (DMSO versus BACE2i 3I proteomic analysis)

ABSTRACT: proteomic analysis of melanoma, PDAC cells and fibroblast treated with DMSO vs 3I

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Malignant Cell, Fibroblast

SUBMITTER: vittoria matafora

LAB HEAD: Angela Bachi

PROVIDER: PXD058789 | Pride | 2026-02-09

REPOSITORIES: Pride

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			Action	DRS
	AE_BXPC3_3I1.raw	Raw
	AE_BXPC3_3I1r.raw	Raw
	AE_BXPC3_3I2.raw	Raw
	AE_BXPC3_3I2r.raw	Raw
	AE_BXPC3_DMSO1.raw	Raw

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Publications

BACE2 tunes lipid uptake through lipid transporters shedding supporting cancer cell proliferation.

Matafora Vittoria V Elhagh Alice A Morelli Alessandra A Tronci Laura L Cattaneo Angela A Conti Camilla C Casagrande Francesca F Farris Francesco F Bachi Angela A

Journal of experimental & clinical cancer research : CR 20260108 1

BACKGROUND: Lipids play crucial roles in signal transduction, membrane integrity, and energy metabolism. In cancer, lipid metabolism is frequently dysregulated. Proliferating cancer cells exhibit enhanced lipid uptake, synthesis, and storage; however, the molecular mechanisms driving cancer metabolic reprogramming remain poorly understood. In this study, we identify Beta-secretase 2 (BACE2), a sheddase overexpressed in several solid tumors, as a critical regulator of lipid metabolism, revealing ...[more]

PMID: 41507981

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Chemoproteomic Approach for Identifying Nuclear Arsenite-binding Proteins

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Quantitative RNA interactome capture (qRIC) identifies phosphorylation sites with regulatory potential - RBM20 BioID

Project description:RNA binding proteins (RBPs) are major regulators of gene expression at the post-transcriptional level. While many posttranslational modification sites in RBPs have been identified, less is known about how these modifications regulate RBP function. Here, we develop quantitative RNA-interactome capture (qRIC) to quantify the fraction of cellular RBPs pulled down with polyadenylated mRNAs. Applying qRIC to HEK293T cells quantified pulldown efficiencies of over 300 mRBPs. Combining qRIC with phosphoproteomics allowed us to systematically compare pulldown efficiencies of phosphorylated and non-phosphorylated forms of mRBPs. Over hundred phosphorylation sites show increased or decreased pull-down efficiency compared to their host RBPs and thus have regulatory potential. Our data captures known regulatory phosphorylation sites in ELAVL1, SF3B1 and UPF1 and identifies new potentially regulatory sites. Follow-up experiments on the cardiac splicing regulator RBM20 revealed that multiple phosphorylation sites in the C-terminal disordered region affect nucleo-cytoplasmic shuttling, association with cytosolic RNA granules and alternative splicing. Together, we show that qRIC is a scalable method to identify the function of posttranslational modifications in RBPs.

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Paradiplonema papillatum CENPA-V5 IP

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Hypolipidemic effects of beetroot juice in SHR-CRP and HHTg rat models of metabolic syndrome: Analysis of hepatic proteome.

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