9.B.230. The GSH-induced LITAF Domain Protein (GILP) Family
Lipopolysaccharide-induced tumor necrosis factor-α (LITAF) is a membrane protein that is highly dependent on correct location to exert transcription factor activity and protein quality control. In humans, LITAF, PIG7 (p53-inducible gene 7), and SIMPLE (small integral membrane protein of the lysosome/late endosome) refer to the same gene, which acts as a tumor suppressor. Several studies have shown that the transcription factor activity and nuclear translocation of the LITAF protein are critical for the induction of several immune cells via classical pathways. In plants, LITAF protein corresponds to the plasma membrane protein AtGILP (Arabidopsis thaliana GSH-induced LITAF domain protein). Cabreira-Cagliari et al. 2017 investigated the LITAF-containing proteins, GILP proteins, in Viridiplantae. They identified 59 genes in 46 species, whose gene copies range from one to three. Phylogenetic analysis showed that multiple copies were originated via block duplication posteriorly to the monocot and eudicot separation. Analysis of the LITAF domain of GILP proteins allowed the identification of a putative domain signature in Viridiplantae, containing a CXXCX41HXCPXC motif. The subcellular location for the majority of GILP proteins was predicted to be in the plasma membrane, based on a transmembrane domain positioned within the LITAF domain. In silico analysis showed that the GILP genes are neither tissue-specific nor ubiquitously expressed, being responsive to stress conditions. Finally, investigation of the GILP protein network resulted in the identification of genes whose families are known to be involved with biotic and/or abiotic stress responses (Cabreira-Cagliari et al. 2017).
The GSH-induced LITAF domain protein, GILP, of 134 aas and 2 TMSs. Acts as a membrane anchor, bringing other regulators of programmed cell death (PCD) to the plasma membrane. It negatively regulates hypersensitive cell death (He et al. 2011). The LITAF domain in GILP localizes in the plasma membrane, interacts with the LSD1 protein, and is involved in negatively regulating PCD.
GILP of Arabidopsis thaliana (Mouse-ear cress)
Uncharacterized protein of 153 aas and 1 TMS.
UP of Aspergillus niger
Lipopolysaccharide-induced tumor necrosis factor-alpha factor homolog, GILP, of 134 aas and 1 TMS.
GILP of Anoplopoma fimbria (Sablefish)
Uncharacterized protein of 205 aas and 1 TMS.
UP of Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)