{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPEX5 is a multifunctional peroxisomal receptor that plays a central role in the import of matrix proteins into peroxisomes. In the cytosol, PEX5 recognizes newly synthesized proteins harboring a type‐1 peroxisomal targeting signal (PTS1) (and, via its longer isoform, PTS2 complexes) and shuttles them to the peroxisomal membrane. Upon docking with membrane‐integrated components—most notably PEX14—PEX5 undergoes conformational changes and is inserted into the docking/translocation machinery. Cargo release correlates with PEX5 cycling, a process that requires receptor monoubiquitination on a conserved cysteine residue and an ATP‐dependent receptor export mediated by AAA ATPases such as PEX1/PEX6; further, the flexible, natively unfolded N-terminal region of PEX5 contributes to these dynamic interactions and receptor recycling. Additionally, PEX5 can modulate alternative processes such as pexophagy by engaging with kinase effectors in response to reactive oxygen species, demonstrating a direct link between peroxisomal protein import and cellular redox homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical transport function, the activity of PEX5 is intricately regulated by posttranslational modifications and interactions that influence both its cargo binding and recycling steps. A conserved cysteine residue in PEX5 serves as a redox switch—its modification under oxidative conditions can impede ubiquitination and thereby alter import efficiency. The existence of distinct isoforms (with PEX5L uniquely facilitating PTS2 import together with PEX7) together with ancillary binding sites and novel PEX14‐interaction motifs underscores how subtle structural elements of PEX5 determine cargo affinity and the kinetics of receptor recycling. Moreover, regulated deubiquitination by enzymes such as USP9X, as well as modulation by chaperones and by interactions with components of the docking/translocation module, further ensure that PEX5 adapts to changing cellular needs, including the activation of autophagy pathways."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMutations or functional perturbations in PEX5 can cause severe peroxisomal biogenesis disorders, underscoring its critical role in organelle homeostasis. Detailed mutational analyses have revealed that defects in PEX5 can lead to selective import deficiencies for PTS1 or PTS2 proteins and are associated with disease phenotypes. Complementing experimental studies, computational models and in vitro reconstitution assays have further refined our understanding of the PEX5 cycle—illustrating how its monoubiquitinated form engages the docking complex, how ancillary cargo binding sites contribute to high‐affinity interactions, and even how competition with other PEX14 ligands (including microtubule‐associated proteins and receptors for other cargos) may influence peroxisomal positioning and function. In addition, physical interactions between PEX5 and other membrane proteins, such as SR-BI, highlight emerging roles for PEX5 beyond protein import."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Jiangwei Zhang, Durga Nand Tripathi, Ji Jing, et al. 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