The RalA binding protein 1 (RalBP1, RLIP1 or RLIP76) multidrug exporter of 655 aas and 2 or 3 TMSs between residues 310 and 370 (Awasthi et al., 2000; Sharma et al., 2001; Awasthi et al., 2007). RLIP76 mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes (Sharma et al. 2001). It can thus catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. The RLIP76 Ral binding domain binds to both the switch regions of RalB, which are the parts of the G protein that change conformation upon nucleotide exchange (Mott and Owen 2010). RLIP76 may play roles in endocytosis, mitochondrial fission, cell spreading and migration, actin dynamics during gastrulation, and Ras-induced tumorigenesis (Goldfinger and Lee 2013). It may additionally serve as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis (Jullien-Flores et al. 1995).  Rlip76 (Rlip) plays roles in ageing and Alzheimer's disease with a focus on oxidative stress and mitochondrial mechanisms (Bandaru et al. 2024).