{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPAK2 is a pivotal serine/threonine kinase that integrates signals from small GTPases to remodel the actin cytoskeleton and govern cell motility. In platelets, its activation by agonists such as thrombin promotes rapid shape changes through the modulation of actin‐binding proteins like cortactin, thereby facilitating lamella and filopodia formation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " In addition, PAK2 regulates focal adhesion dynamics in epithelial and cancer cells by associating with adaptor proteins—for example, βPIX/GIT1 and MYO18A—to fine‐tune cell adhesion and migration, processes that are critical for invasive behaviors observed in breast and prostate carcinomas."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "3", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDepending on its mode of activation, PAK2 exerts contrasting roles in cell fate decisions. Full‐length PAK2 can support survival signaling, whereas its caspase‐cleaved C-terminal fragment is myristoylated and re-localizes to membranes, thereby promoting apoptosis. Moreover, PAK2 phosphorylates key regulatory proteins such as Myc—attenuating its transcriptional and transforming activities—and targets substrates like Mnk1 and eIF4G to couple stress signals with translational inhibition, collectively influencing cell proliferation, cell cycle progression, and apoptotic sensitivity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of infectious diseases and receptor signaling, viral proteins such as HIV-1 Nef engage PAK2 to modulate T cell function and enhance viral infectivity. Specific domains of Nef mediate this association, although the downstream consequences for T-cell activation and apoptosis appear multifaceted. Beyond viral hijacking, PAK2 also regulates receptor-mediated processes—participating in clathrin-independent endocytosis of interleukin-2 receptor β—and modulating responses to growth factors like hepatocyte growth factor, where it influences epithelial scattering and motility. Its interactions extend to key signaling networks, including c-Abl activation and attenuation of TGF-β responses via inhibitory phosphorylation of Smad proteins."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAberrant PAK2 signaling is implicated in tumor progression and metastasis across several cancers. In pancreatic ductal adenocarcinoma, for example, metabolic regulators such as PKM2 directly phosphorylate PAK2, thereby stabilizing it and promoting metastatic behaviors. Conversely, tumor-suppressive microRNAs (e.g., miR-137, miR-134, and miR-4779) have been shown to target PAK2, resulting in reduced cell proliferation and increased chemosensitivity in melanoma, ovarian, and colon cancers. Furthermore, PAK2 operates downstream of tumor suppressor pathways such as TSC1/2-RHEB and is modulated by kinases like CDK12 to activate MAPK signaling in gastric cancer, underscoring its role as a key effector in oncogenic networks."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "22", "end_ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPAK2 additionally contributes to the proper progression of mitosis and the maintenance of cellular homeostasis. It is activated at centrosomes in a Rac1-dependent manner and participates in regulating centrosome separation during early mitosis, thereby ensuring accurate chromosome segregation. Beyond its mitotic role, PAK2 influences cellular aging by modulating histone H3.3 deposition and gene expression programs required for the establishment of senescence."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "28", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Catherine Vidal, Blandine Geny, Josiane Melle, et al. 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