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The Phosphorylation Landscape of Interferon-Induced Antiviral Signaling

ABSTRACT: Phosphorylation events act as a fine switch that regulates the proper functioning of the innate immune system upon IFN stimulation. Upon binding of IFN to its receptor, phosphorylation and activation of the Jak/STAT pathway is a very well studied event. However, little is known about the activation of other pathways and the role they play in modulating this powerful antiviral response. This led us to raise the hypothesis that, changes in the phosphorylation status of proteins induced by IFN stimulation can activate novel signaling pathways with an impact on the IFN response. To this end, we have conducted a label-free quantitative phosphoproteomic analysis and identified a new set of proteins that are modified upon IFN treatment, and thereby may represent novel candidates acting at different levels of the IFN response.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

SUBMITTER: Idoia Busnadiego

LAB HEAD: Prof. Dr. Benjamin G. Hale

PROVIDER: PXD029969 | Pride | 2025-03-10

REPOSITORIES: Pride

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			Action	DRS
	20170904_06_control_R1_30min_IMAC.raw	Raw
	20170904_07_gamma_R2_30min_IMAC_11.raw	Raw
	20170904_08_beta_R4_30min_IMAC_21.raw	Raw
	20170904_09_lamda_R4_30min_IMAC_24.raw	Raw
	20170904_10_omega_R1_30min_IMAC_4.raw	Raw

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