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BACE2 and lipid metabolism (global proteomic analysis)

ABSTRACT: global proteomic analysis of melanoma cell lines expressing different bace2 levels

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: vittoria matafora

LAB HEAD: Angela Bachi

PROVIDER: PXD058702 | Pride | 2026-02-09

REPOSITORIES: Pride

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			Action	DRS
	CC_115_1.raw	Raw
	CC_115_1r.raw	Raw
	CC_115_2rr.raw	Raw
	CC_115_2rrr.raw	Raw
	CC_115_3r.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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Transcriptome analysis after BACE2 silencing in ocular melanoma cella

Project description:In order to study the mechanism of BACE2 and the development of melanoma, we established a model of low expression of BACE2 in melanoma. The results showed that the expression of tmem38b was decreased after BACE2 knockdown, and the intracellular calcium concentration was decreased. In order to reveal the interaction between BACE2 and tmem38b and the effect of intracellular Ca2 + concentration on the formation and development of melanoma, and to further explore BACE2 The relationship between the expression level and the survival time of OM patients provides new ideas for the treatment of malignant tumors

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Chemoproteomic Approach for Identifying Nuclear Arsenite-binding Proteins

Project description:Trivalent arsenic [As(III)], the predominant environmental form, poses significant health risks, including cancer, diabetes, and cardiovascular and neurodegenerative diseases, through contaminated food and water ingestion. Studies have explored As(III) toxicity mechanisms, particularly its displacement of Zn(II) in zinc-binding proteins, but identifying direct As(III)-binding proteins remains crucial. Given the nucleic acid binding capacity of many zinc-binding proteins, we hypothesized that nuclear As(III)-binding proteins could reveal key toxicity targets. Using a quantitative proteomics approach, we performed affinity pull-down with a biotin-As(III) probe on nuclear protein lysate. We identified splicing factor 1 (SF1) as a direct As(III)-binding protein and demonstrated that this interaction modulates mRNA splicing in human cells.

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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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