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Proteomics analysis of tissue aging nucleic acid binding proteins

ABSTRACT: The landscape of NABPs in different mouse stage will assist in the greater understanding of the cellular and molecular mechanisms which control immune system development and aging.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Spleen, Lung, Kidney

SUBMITTER: Huiyu Wang

LAB HEAD: Hua Xiao

PROVIDER: PXD035405 | Pride | 2026-03-04

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	2021806-YP202139351-xh-kidney-nucl1.raw	Raw
	2021806-YP202139351-xh-kidney-nucl2.raw	Raw
	2021806-YP202139351-xh-kidney-nucl3.raw	Raw
	2021806-YP202139351-xh-kidney-total1.raw	Raw
	2021806-YP202139351-xh-kidney-total2.raw	Raw

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Publications

Deciphering Nucleic Acid Binding Proteome of Mouse Immune Organs Reveals Hub Proteins for Aging.

Wang Huiyu H Zhang Yan Y Wang Zeyuan Z Zhang Lu L Guo Miao M Cao Chengxi C Xiao Hua H

Molecular & cellular proteomics : MCP 20230628 8

Profiling the nucleic acid-binding proteins (NABPs) during aging process is critical to elucidate its roles in biological systems as well as transcriptional and translational regulation. Here, we developed a comprehensive strategy to survey the NABPs of mouse immune organs by using single cell preparation and selective capture technology-based proteomics. Our approach provided a global view of tissue NABPs from different organs under normal physiological conditions with extraction specificity of ...[more]

PMID: 37391046

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Proteomics analysis of tissue aging nucleic acid binding proteins

Project description:The landscape of NABPs in different mouse stage will assist in the greater understanding of the cellular and molecular mechanisms which control immune system development and aging.

2026-03-04 | PXD035412 | Pride

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Targeting microRNA-dependent control of X chromosome inactivation improves the Rett Syndrome phenotype

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2026-02-09 | PXD064749 | Pride

Juxtaposition of Bub1 and Cdc20 on phosphorylated Mad1 during catalytic mitotic checkpoint complex assembly (IGX-MS data)

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Dynamic phosphoproteomics of BRS3 activation reveals Hippo signaling pathway for cell migration

Project description:Bombesin receptor subtype-3 (BRS3) is an orphan G-protein coupled receptor (GPCR) that involved in a range of pathological and physiological processes, while its biological functions and underlying regulatory mechanisms remain largely unknown. Quantitative phosphoproteomics approach was employed in this study to comprehensively decipher the signal transductions that occurred upon intracellular BRS3 activation. Lung cancer cell line H1299-BRS3 was treated with MK-5046, an agonist of BRS3, for different durations. Harvested cellular proteins were digested and phosphopeptides were enriched by immobilized titanium (IV) ion affinity chromatography (Ti4+-IMAC) for label-free quantification analysis. In total, 12,052 phosphopeptides were identified, corresponding to 4,015 phosphoproteins and 10,820 phosphosites. Data analysis revealed that 27 phosphopeptides corresponding to 6 proteins were involved in Hippo signaling pathway, which was significantly regulated by the activation of BRS3. Verification experiments demonstrated down-regulation of Hippo signaling pathway could induce the dephosphorylation and nucleus localization of Yes-associated protein (YAP), which further confirmed its association with cell migration through kinase inhibition. Our data collectively demonstrate that BRS3 activation contributes to cell migration through down-regulating Hippo signaling pathway.

2023-07-12 | PXD035666 | Pride

Detecting differential peaks in ChIP-seq signals with ODIN

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Integrative Structural Characterization of the Human Canonical and Non-canonical Cop9 Signalosome Complexes

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