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Alterations in proteome and proteostasis networks during replicative senescence

ABSTRACT: The accumulation of senescent cells constitutes a pivotal hallmark of tissue ageing, contributing to disruption of tissue homeostasis and thus, to the development of several aging-related diseases. Despite this, our knowledge about the molecular, spatial and temporal changes that drive aging on a cellular basis remains poorly understood. To elucidate these mechanisms, we employed mass spectrometry-based proteomics to determine changes in the proteome and its post translational modifications, as well as protein solubility, during replicative senescence in human IMR90 fibroblasts. This accession contains data regarding alterations on the ubiquitin-modified proteome, in control and Bortezomib-treated conditions.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Fibroblast Of Lung

SUBMITTER: Petra Beli

LAB HEAD: Petra Beli

PROVIDER: PXD077923 | Pride | 2026-07-16

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	01_14_2026_14_56_51_LOG_OtUBD_input.txt	Txt
	01_14_2026_14_56_51_log_OtUBD_pulldown_Bortezomib.txt	Txt
	20260123_AST1_PBE_NS_IMR90_OtUBD_input_Bortezomib_Proliferative_R1.raw	Raw
	20260123_AST1_PBE_NS_IMR90_OtUBD_input_Bortezomib_Proliferative_R2.raw	Raw
	20260123_AST1_PBE_NS_IMR90_OtUBD_input_Bortezomib_Proliferative_R3.raw	Raw

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Alterations in proteome and proteostasis networks during replicative senescence

Project description:The accumulation of senescent cells constitutes a pivotal hallmark of tissue ageing, contributing to disruption of tissue homeostasis and thus, to the development of several aging-related diseases. Despite this, our knowledge about the molecular, spatial and temporal changes that drive aging on a cellular basis remains poorly understood. To elucidate these mechanisms, we employed mass spectrometry-based proteomics to determine changes in the total proteome, the ubiquitin-modified proteome, the phospho-proteome and in protein solubility during replicative senescence in human IMR90 fibroblasts. This accession contains data of the ubiquitin-modified proteome.

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