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. 2020 Oct 5;10:16501. doi: 10.1038/s41598-020-73552-9

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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CD300e working model. (a) The binding of IFN-γ to the interferon-gamma-receptor (IFNGR) leads to the dimerization of the receptor, activation of JAK1 and JAK2, recruitment and phosphorylation of STAT1. Following dimerization, phosphorylated STAT1 enters the nucleus and transcribes target genes, including STAT1 and CIITA, the master control regulator of HLA-II expression. (b) The engagement of CD300e in monocytes thwarts the basal expression of STAT1. Therefore, the unphosphorylated STAT1-dependent expression of CIITA is hampered, and in turn that of HLA-II. (c) The activation through CD300e, even under IFN-γ induction, keeps low the transcription of STAT1 gene, thus lowering the amount of STAT1 available for activation by phosphorylation. This, in turn, results in an impairment of CIITA and HLA-II synthesis. RFX, NFY and CREB are part of the heteromultimeric scaffold required for CIITA transcriptional activity.