{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nProfilin 2 (PFN2) is a multifunctional actin‐binding protein that plays a central role in regulating actin dynamics and cytoskeletal remodeling. At the biochemical level, PFN2 participates in the control of actin polymerization and interacts with numerous partners, including regulators of actin acetylation and Rho‐dependent kinases, thereby influencing protein aggregation processes as seen in neurodegenerative disease models. In addition, PFN2 activity is finely modulated by post‐translational modifications – for example, phosphorylation events can act as molecular switches to alter its affinity for actin and poly‐L‐proline ligands, while its ubiquitination by specific E3 ligases further tunes its cellular concentrations. Emerging evidence also indicates that PFN2 is implicated in stem cell biology by influencing endocytosis and signal transduction cascades that govern proliferation and differentiation. Collectively, these studies underscore a fundamental role for PFN2 in orchestrating cytoskeletal homeostasis and signal integration."}, {"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 the context of cancer, PFN2 exerts complex, sometimes contrasting roles that appear to be highly context‐ and tissue‐dependent. In lung, head and neck, small cell lung, triple‐negative breast, prostate, and gastric cancers, upregulated PFN2 promotes tumor progression by enhancing epithelial–mesenchymal transition, cell migration, invasion, and stemness through modulation of key signaling pathways such as TGF‑β/Smad, PI3K/Akt/β‐catenin, and ERK, as well as through epigenetic and noncoding RNA–mediated mechanisms. Conversely, in certain cancers such as colorectal and oral squamous cell carcinoma, diminished PFN2 levels have been associated with enhanced migratory properties and poorer prognosis, suggesting a possible tumor‐suppressive function. Moreover, PFN2 has been implicated in oncogenic Ras signaling via its interaction with RalGDS‐related proteins and may be regulated by competing endogenous RNA networks. These findings reveal that PFN2 is embedded in a complex regulatory network in tumorigenesis, serving both as a potential driver of malignant progression and as a prognostic biomarker."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in cytoskeletal regulation and cancer, PFN2 has emerged as a relevant player in several other pathological and physiological contexts. In diabetic nephropathy and glomerular diseases such as focal segmental glomerulosclerosis, PFN2 is transcriptionally modulated to impact endothelial‐to‐mesenchymal transition and actin turnover, while alterations in its interaction with disease‐linked proteins may contribute to podocyte dysfunction. In addition, PFN2 appears to influence trophoblast migration in preeclampsia via regulation by microRNAs and is targeted by viral proteins during infections to promote F‐actin reorganization that facilitates viral growth. Finally, molecular signatures implicating PFN2 have also been identified in inherited neuropathies, highlighting its potential as a broader disease marker. These studies indicate that PFN2 is a pivotal component in diverse cellular circuits, with emerging relevance as both a prognostic indicator and therapeutic target."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "26", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Jieya Shao, William J Welch, Nicholas A Diprospero, et al. 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