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Phosphoproteomics combined with quantitative 14-3-3-affinity capture identifies SIRT1 and RAI as new regulators of cytosolic dsRNA-induced innate immune response

ABSTRACT: In this study, we have used global phosphoproteomic analysis to define phosphorylation-dependent signaling events regulated during RLR stimulation in human keratinocytes. In addition, we used quantitative 14-3-3-affinity capture to identify major target molecules of 14-3-3 regulation.

INSTRUMENT(S): QSTAR

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Keratinocyte

SUBMITTER: Tuula Nyman

LAB HEAD: Tuula Nyman

PROVIDER: PXD000670 | Pride | 2014-07-08

REPOSITORIES: Pride

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Phosphoproteomics combined with quantitative 14-3-3-affinity capture identifies SIRT1 and RAI as novel regulators of cytosolic double-stranded RNA recognition pathway.

Öhman Tiina T Söderholm Sandra S Hintsanen Petteri P Välimäki Elina E Lietzén Niina N MacKintosh Carol C Aittokallio Tero T Matikainen Sampsa S Nyman Tuula A TA

Molecular & cellular proteomics : MCP 20140705 10

Viral double-stranded RNA (dsRNA) is the most important viral structure recognized by cytosolic pattern-recognition receptors of the innate immune system, and its recognition results in the activation of signaling cascades that stimulate the production of antiviral cytokines and apoptosis of infected cells. 14-3-3 proteins are ubiquitously expressed regulatory molecules that participate in a variety of cellular processes, and 14-3-3 protein-mediated signaling pathways are activated by cytoplasmi ...[more]

PMID: 24997996

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14-3-3 affinity capture to identify new targets of 14-3-3 signaling during dsRNA-stimulation in human keratinocytes.

Project description:We have combined two proteomic approaches, phosphoproteomics and 14-3-3 affinity capture, to examine the signaling pathways in which 14-3-3 proteins participate and to identify new targets of 14-3-3 signaling during dsRNA-stimulation.

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Vitrification of embryos modifies foetal placenta proteome. LCMSMS

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