Proteomics

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Quantification on NOD1 ubiquitination sites with ubiquitin and SspH2 co-overexpression


ABSTRACT: HEK293T cells were transiently transfected with NOD1-FLAG, HA-SspH2 WT/HA-SspH2 C580/empty vector, and Myc-Ubiquitin. Following anti-FLAG automated immunoprecipitation and in-gel trypsin digestion, fractionated samples were injected onto LC-MS/MS. Quantitation was performed on diglycyl-lysine sites on NOD1, on identical peptides with highest intensity across samples.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Olivier Julien   Amit Bhavsar  

PROVIDER: MSV000087693 | MassIVE | Wed Jun 23 16:43:00 BST 2021

REPOSITORIES: MassIVE

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Publications

The <i>Salmonella</i> Effector SspH2 Facilitates Spatially Selective Ubiquitination of NOD1 to Enhance Inflammatory Signaling.

Delyea Cole J CJ   Forster Malcolm D MD   Luo Shu S   Dubrule Bradley E BE   Julien Olivier O   Bhavsar Amit P AP  

Biochemistry 20240827 18


As part of its pathogenesis, <i>Salmonella enterica</i> serovar Typhimurium delivers effector proteins into host cells. One effector is SspH2, a member of the so-called novel E3 ubiquitin ligase family, that interacts with and enhances, NOD1 pro-inflammatory signaling, though the underlying mechanisms are unclear. Here, we report that SspH2 interacts with multiple members of the NLRC family to enhance pro-inflammatory signaling by targeted ubiquitination. We show that SspH2 modulates host innate  ...[more]

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