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Effect of heat-shock on total, poly-ubiquitylated, and insoluble proteomes of human IMR-90 fibroblasts in different proliferation states

ABSTRACT: Cellular stress responses are crucial for survival in sub-optimal conditions, and almost invar-iably involve proteome-wide alterations at the levels of protein abundance, post-translational modification with poly-ubiquitin chains (poly-ubiquitylation), and solubility. However, most of our understanding of human cell stress responses at the protein level stems from experi-ments in rapidly-dividing cell culture models. Here, we used primary human diploid lung fibro-blasts (IMR-90) in proliferating, contact-inhibited quiescent, or doxorubicin-induced senes-cent states, to explore their responses to a severe heat-shock (44 degrees Celsius for 2 hours) at the total, poly-ubiquitylated, and insoluble proteome levels.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Fibroblast

SUBMITTER: Harvey Johnston

LAB HEAD: Rahul Samant

PROVIDER: PXD067225 | Pride | 2025-10-08

REPOSITORIES: Pride

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			Action	DRS
	File_description_summary.xlsx	Xlsx
	IMR90_heat-shock.sdrf.xlsx	Xlsx
	Ref_1002-10_FAIMS_RTS_MS3.raw	Raw
	Ref_1002-11_FAIMS_RTS_MS3.raw	Raw
	Ref_1002-12_FAIMS_RTS_MS3.raw	Raw

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