| http://purl.uniprot.org/citations/28377411 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/28377411 | http://www.w3.org/2000/01/rdf-schema#comment | "The ability to tune cellular functions in response to nutrient availability has important consequences for immune homeostasis. The activity of the receptor Notch in regulatory T (Treg) cells, which suppress the functions of effector T cells, is indispensable for Treg cell survival under conditions of diminished nutrient supply. Anti-apoptotic signaling induced by the Notch1 intracellular domain (NIC) originates from the cytoplasm and is spatially decoupled from the nuclear, largely transcriptional functions of NIC. We showed that Sirtuin 1 (Sirt1), which is an NAD+ (nicotinamide adenine dinucleotide)-dependent lysine deacetylase that inhibits NIC-dependent gene transcription, stabilized NIC proximal to the plasma membrane to promote the survival and function of activated Treg cells. Sirt1 was required for NIC-dependent protection from apoptosis in cell lines but not for the activity of the anti-apoptotic protein Bcl-xL. In addition, a variant NIC protein in which four lysines were mutated to arginines (NIC4KR) retained anti-apoptotic activity, but was not regulated by Sirt1, and reconstituted the functions of nonnuclear NIC in Notch1-deficient Treg cells. Loss of Sirt1 compromised Treg cell survival, resulting in antigen-induced T cell proliferation and inflammation in two mouse models. Thus, the Sirt1-Notch interaction may constitute an important checkpoint that tunes noncanonical Notch1 signaling."xsd:string |
| http://purl.uniprot.org/citations/28377411 | http://purl.org/dc/terms/identifier | "doi:10.1126/scisignal.aah4679"xsd:string |
| http://purl.uniprot.org/citations/28377411 | http://purl.uniprot.org/core/author | "Shukla S.K."xsd:string |
| http://purl.uniprot.org/citations/28377411 | http://purl.uniprot.org/core/author | "Marcel N."xsd:string |
| http://purl.uniprot.org/citations/28377411 | http://purl.uniprot.org/core/author | "Sarin A."xsd:string |
| http://purl.uniprot.org/citations/28377411 | http://purl.uniprot.org/core/author | "Perumalsamy L.R."xsd:string |
| http://purl.uniprot.org/citations/28377411 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
| http://purl.uniprot.org/citations/28377411 | http://purl.uniprot.org/core/name | "Sci Signal"xsd:string |
| http://purl.uniprot.org/citations/28377411 | http://purl.uniprot.org/core/pages | "eaah4679"xsd:string |
| http://purl.uniprot.org/citations/28377411 | http://purl.uniprot.org/core/title | "The lysine deacetylase Sirtuin 1 modulates the localization and function of the Notch1 receptor in regulatory T cells."xsd:string |
| http://purl.uniprot.org/citations/28377411 | http://purl.uniprot.org/core/volume | "10"xsd:string |
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