{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n ACAP1 is an ADP‐ribosylation factor (Arf) GTPase‐activating protein (GAP) that primarily acts on Arf6, thereby controlling the activity of this key regulator of membrane trafficking. Early studies demonstrated that ACAP1, along with the closely related ACAP2, is recruited to peripheral membranes where it preferentially inactivates Arf6; this inactivation is critical for inhibiting the formation of PDGF‐induced dorsal ruffles and for controlling the generation of Arf6‐dependent membrane protrusions (1,2). Subsequent work revealed that ACAP1 is a multifunctional adaptor within a clathrin coat complex that mediates endocytic recycling events. For example, ACAP1 specifically binds to cargo proteins such as the transferrin receptor by recognizing recycling sorting signals, thereby promoting their proper sorting from the recycling endosome (3,4). Its role is further expanded by cooperating with phosphoinositide kinases to induce the formation of endosomal tubules, a process that requires the structural integrity of both its BAR and PH domains (5). Moreover, ACAP1 is critical for the regulated recycling of integrins and GLUT4-containing vesicles, processes that are modulated by phosphorylation through the Akt pathway; phosphorylation relieves an autoinhibitory mechanism to enhance cargo binding and ensure efficient recycling toward the plasma membrane (6,7). In neuronal cells, inactivation of Arf6 by ACAP1 increases recycling of β1 integrins to the cell surface, thereby favoring anterograde transport and promoting axon growth (10). In addition to its well‐defined roles in regulating endocytic recycling and cell migration, altered ACAP1 expression has been linked to pathophysiological conditions including Alzheimer’s disease and certain cancers, where its decreased or aberrant expression correlates with disease progression (8,9). Finally, ACAP1 has also been implicated in pathogen–host interactions; for instance, a bacterial effector (BspF) can interact with ACAP1 to dysregulate recycling endosome dynamics, ultimately promoting intracellular bacterial replication (11)."}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "b", "children": [{"type": "t", "text": "Citations:"}]}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "T R Jackson, F D Brown, Z Nie, et al. 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