Abstract
Cellular inhibitor of apoptosis 1 (cIAP1) is a cell signaling regulator of the IAP family. Through its E3-ubiquitine ligase activity, it has the ability to activate intracellular signaling pathways, modify signal transduction pathways by changing protein-protein interaction networks, and stop signal transduction by promoting the degradation of critical components of signaling pathways. Thus, cIAP1 appears to be a potent determinant of the response of cells, enabling their rapid adaptation to changing environmental conditions or intra- or extracellular stresses. It is expressed in almost all tissues, found in the cytoplasm, membrane and/or nucleus of cells. cIAP1 regulates innate immunity by controlling signaling pathways mediated by tumor necrosis factor receptor superfamily (TNFRs), some cytokine receptors and pattern recognition-receptors (PRRs). Although less documented, cIAP1 has also been involved in the regulation of cell migration and in the control of transcriptional programs.
Highlights
IAPs (Inhibitors of Apoptosis) form a family of proteins highly conserved during evolution
In a work published in 2004, we demonstrated that Cellular inhibitor of apoptosis 1 (cIAP1) is expressed in the nucleus of hematopoietic stem cells [50], and that its translocation into the cytoplasm is necessary for their differentiation into macrophages or dendritic cells [21,45,50]
Gene expression profiling interactive analysis (GEPIA) [54] revealed that cIAP1 expression tends to be overexpressed in 11 out of 31 tumors selected in the cancer genome atlas (TCGA), which is significant for diffuse large B-cell lymphoma (DLBC), glioblastoma multiforme (GBM) and thymoma (THYM) (Figure 3)
Summary
IAPs (Inhibitors of Apoptosis) form a family of proteins highly conserved during evolution. The BIR1 of cIAP1/2 binds the signaling adaptor tumor necrosis factor receptor (TNFR)-associated factor 2 (TRAF2) (Figure 1) which regulates the stability, localization and activity of the concerned IAPs and which acts as an intermediate for their recruitment into TNFR-associated signaling complex [27–29]. IAPs bind, via the Ring, ubiquitin-charged E2-conjugating enzyme and catalyze the transfer of ubiquitin moieties from the E2 to the protein substrate, recruited thanks to their BIR domains [15]. In addition to the BIRs and Ring, cIAPs and XIAP harbor a UBA (ubiquitin- associated) domain whose function is to bind ubiquitins [40,41] (Figure 1). It has been involved in regulating cIAPs-mediated ubiquitination.
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