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RalB also contributes to normal immune cell function by mediating chemokine‐induced migration in B cells and multiple myeloma."}, {"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": "\nBeyond its role in oncogenic survival, RalB regulates key membrane trafficking and cytoskeletal events that underlie autophagy, cell division, and invasion. Upon nutrient deprivation, RalB is activated and localizes to nascent autophagosomes where, via binding to the effector Exo84, it orchestrates the assembly of ULK1 and Beclin1‐VPS34 complexes essential for autophagosome formation. RalB also directs cytokinetic abscission by recruiting the exocyst to the midbody, and it promotes invadopodia formation that drives matrix remodeling and cell invasion. Post‐translational modifications such as phosphorylation at Ser198 by PKC modulate RalB’s subcellular localization and effector engagement, while interactions with molecules like calmodulin and Arf6 fine‐tune its role in directional trafficking and membrane fusion."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to these functions, RalB plays pivotal roles in normal cellular and immune processes and in the modulation of oncogenic signaling circuits. In natural killer cells, for instance, rapid RalB activation upon target recognition governs degranulation and effective cytotoxic responses. Its activity is also precisely controlled by post‐translational mechanisms—including ubiquitylation and prenylation—that dictate its subcellular partitioning and effector specificity. 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