Matches in SemOpenAlex for { <https://semopenalex.org/work/W4382632488> ?p ?o ?g. }
- W4382632488 abstract "Src is a protein tyrosine kinase commonly activated downstream of transmembrane receptors and plays key roles in cell growth, migration, and survival signaling pathways. In conventional dendritic cells (cDCs), Src is involved in the activation of the non-enzymatic functions of indoleamine 2,3-dioxygenase 1 (IDO1), an immunoregulatory molecule endowed with both catalytic activity and signal transducing properties. Prompted by the discovery that the metabolite spermidine confers a tolerogenic phenotype on cDCs that is dependent on both the expression of IDO1 and the activity of Src kinase, we here investigated the spermidine mode of action. We found that spermidine directly binds Src in a previously unknown allosteric site located on the backside of the SH2 domain and thus acts as a positive allosteric modulator of the enzyme. Besides confirming that Src phosphorylates IDO1, here we showed that spermidine promotes the protein–protein interaction of Src with IDO1. Overall, this study may pave the way toward the design of allosteric modulators able to switch on/off the Src-mediated pathways, including those involving the immunoregulatory protein IDO1." @default.
- W4382632488 created "2023-07-01" @default.
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- W4382632488 date "2023-06-30" @default.
- W4382632488 modified "2023-10-18" @default.
- W4382632488 title "A back-door insight into the modulation of Src kinase activity by the polyamine spermidine" @default.
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- W4382632488 doi "https://doi.org/10.7554/elife.85872" @default.
- W4382632488 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37387273" @default.
- W4382632488 hasPublicationYear "2023" @default.
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