{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRALBP1 (also known as RLIP76) is a multifunctional protein that plays central roles in the regulation of intracellular signaling and membrane dynamics. It functions as an effector for Ral small GTPases and participates in mitotic events by coordinating mitochondrial fission, proper centrosome separation, and the shutdown of clathrin‐dependent endocytosis. In dividing cells, for example, phosphorylation events mediated by kinases such as Aurora A and cyclin B–CDK1 help redistribute RALBP1 (via its binding partner RALA) to the mitochondria and centrosomes, thereby ensuring proper segregation of organelles and modulating cell cycle progression. Furthermore, interactions with proteins like cdc2 and stress‐responsive transcription factors (e.g. Hsf‑1) modulate its transport functions and, in doing so, influence signaling cascades that control cell survival and p27 localization."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its regulatory roles in cell division and cytoskeletal organization, RLBP1 is a high‐capacity, ATP‑dependent transporter for glutathione conjugates of endogenous electrophiles and various xenobiotics including chemotherapeutic agents such as doxorubicin. Its intrinsic ATPase activity is stimulated by these substrates, and post‑translational modifications (for example, phosphorylation by PKCα at specific sites) further modulate its transport function. This transport activity not only underlies a cellular defense mechanism against oxidative and electrophilic stress but also contributes substantially to drug resistance observed in several solid tumors and hematological malignancies."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in cell division and xenobiotic transport, RLBP1 is intimately linked to cancer progression and metastasis. It acts as a nodal point integrating various signaling pathways that regulate apoptosis, cell migration, and invasion. Alterations in its expression or function—influenced by interactions with binding partners such as POB1, regulation by microRNAs (for example, miR‑101 and miR‑143‑3p), and control at the transcriptional level by coactivators like p300—can promote oncogenic processes across diverse tumor types including prostate, breast, colorectal, glioma, gastric, ovarian, and melanoma. In addition, immune recognition of RLBP1 epitopes has been implicated in vascular and autoimmune dysfunction, and inflammatory mediators may upregulate its expression at barriers such as the blood–brain barrier. Collectively, these multifaceted roles make RLBP1 both a prognostic marker and a promising therapeutic target in cancer and other diseases."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "25", "end_ref": "40"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Carine Rossé, Sébastien L'Hoste, Nicolas Offner, et al. 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