SHP-1 interacts with NFκB1 to inhibit its phosphorylation and nuclear translocation to suppress excessive bacterial inflammation

Abstract excerpt

The protein tyrosine phosphatase SHP-1 is a key negative regulator in cancer by dephosphorylating multiple target molecules. Specially in the NFκB signaling, where NFκB1/Rela dimer translocate to the nucleus and activate target gene transcription, SHP-1 inhibits the phosphorylation of Rela, while its regulation on NFκB1 has been unknown, especially in pathogen-induced inflammation. Chinese tongue sole, a represent...

Topics

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• Calcium signaling and nucleotide metabolism
• Cytokine Signaling Pathways and Interactions
• Cytomegalovirus and herpesvirus research
• Datasets as Topic
• Inflammasome and immune disorders
• interferon and immune responses
• Protein Tyrosine Phosphatases
• RNA Interference and Gene Delivery

Identifiers and source

Literature Corpus work

c6cac0eb-7fcf-53e7-8f05-42baeca63cea

DOI

10.1101/2024.04.13.589348