{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRAB22A functions as a critical regulator of early endosomal dynamics and cargo sorting. It localizes to early and sorting endosomes, where it interacts with effectors such as EEA1 and Rabex‐5, thereby coordinating the maturation and recycling of cargo markers including major histocompatibility complex class I and the transferrin receptor. RAB22A has been shown to participate in the formation of tubular recycling intermediates by bridging complexes (e.g., BLOC‐1/BLOC‐2/KIF13A) and is activated by specific guanine nucleotide exchange factors – recently, Vps9d1 was identified as a dedicated activator ensuring the proper formation of tubular endosomes. In addition, structural domains within RAB22A, such as its interswitch and hypervariable regions, contribute to its precise endosomal targeting and functional interactions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn cancer cells, RAB22A has emerged as an oncogenic player that promotes cell migration, invasion, and metastasis via multiple mechanisms. For example, hypoxic conditions in breast tumors induce its HIF‐dependent upregulation, thereby augmenting the shedding of microvesicles/exosomes that in turn stimulate metastatic behaviors. In several malignancies – including ovarian cancer, melanoma, lung adenocarcinoma, liver and thyroid cancers, and even multiple myeloma – RAB22A is upregulated and its oncogenic activities are further modulated by tumor‐suppressive microRNAs (such as miR‑373, miR‑204, miR‑193b, and miR‑203) that normally target its mRNA expression. In some osteosarcoma studies, fusion proteins incorporating the Rab22a N‑terminus (e.g. Rab22a‑NeoF1) have been shown to drive metastasis through abnormal post‑translational modifications and subsequent activation of RhoA signaling. Moreover, RAB22A supports oncogenic recycling pathways that stabilize cell surface proteins (for instance, CD147 in lung cancer), ultimately contributing to aggressive tumor phenotypes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRAB22A also plays important roles in immune regulation and host–pathogen interactions. It is involved in the intracellular trafficking of pathogens and viral particles – for instance, facilitating the movement of vaccinia virus particles through endosomal compartments prior to uncoating – and in the phagocytic uptake and lysosomal delivery of bacteria such as Borrelia burgdorferi in macrophages. In dendritic cells, RAB22A contributes to efficient antigen cross‑presentation by regulating the recruitment of endoplasmic reticulum components to phagosomes, thereby modulating immune surveillance."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "25", "end_ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional regulatory layers governing RAB22A function have been uncovered. In osteosarcoma, for example, the Rab22a‑NeoF1 fusion protein requires K7 acetylation for its metastasis‑promoting activity, offering a potential therapeutic target. Furthermore, in vascular contexts, a circRNA/miRNA axis (circ‑C16orf62/miR‑377) modulates RAB22A expression to influence macrophage apoptosis, inflammation, oxidative stress, and cholesterol handling during atherosclerosis. Finally, its colocalization with hypoxia‑inducible factors in breast cancer and roles in specialized exocytotic events – as seen in sperm acrosome reactions – underscore its diverse cellular functions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "28", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Roberto Weigert, Albert Chi Yeung, Jean Li, et al. 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