{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nProfilin‑1 (PFN1) is a small yet essential actin‐binding protein that orchestrates actin dynamics by catalyzing the conversion of globular (G)‐actin to filamentous (F)‐actin. It achieves this through direct binding to actin monomers and by serving as an adaptor between actin and numerous ligands—including proline‐rich proteins and phosphatidylinositol lipids—to regulate filament elongation (thereby cooperating with filament elongation factors such as formins and Ena/VASP). PFN1’s interaction interfaces have been mapped structurally, revealing distinct binding sites that mediate its associations with both G‑actin and phosphoinositides, and these interactions are critical not only for cytoskeletal polymerization but also for more specialized functions such as directing nuclear events including pre‑mRNA splicing."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDysfunction of PFN1—arising either from mutations that destabilize its structure or from aberrant regulation—has been implicated in neurodegenerative diseases. In familial amyotrophic lateral sclerosis (ALS) and related motor neuron disorders, specific PFN1 point mutations lead to its misfolding and aggregation, often sequestering other key proteins such as TDP‑43 and thereby perturbing RNA metabolism and stress granule dynamics. Similar PFN1 mutations have been modeled in yeast and transgenic mice, where they drive motor neuron loss and abnormal axonal actin dynamics; in parallel, studies in Huntington’s disease demonstrate that phosphorylated PFN1 impairs aggregate clearance. Collectively, these findings implicate impaired PFN1 function—and the subsequent disruption of cytoskeletal as well as nucleocytoplasmic transport pathways—as a central mechanism in neurodegeneration."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "20"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in neural health, PFN1 plays a critical part in regulating cell motility, proliferation, and adhesion in a variety of cancers and vascular diseases. In several epithelial‐derived tumors—including those of the breast, pancreas, bladder, and liver—altered PFN1 expression has been linked to changes in actin filament organization that affect lamellipodial dynamics, cell–cell as well as cell–matrix adhesion, and ultimately the propensity for invasion and metastasis. In breast cancer models, for instance, reduced PFN1 levels are associated with enhanced cell scattering and invasion, whereas its moderate overexpression can impose growth arrest and even suppress metastatic colonization. PFN1 also influences endothelial cell behavior, contributing to capillary morphogenesis and vascular barrier function, and has been proposed as a biomarker in several malignancies."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "33"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPFN1 is itself subject to tight regulation by posttranslational modifications and protein–protein interactions that modulate its activity in different contexts. Phosphorylation of PFN1—mediated by pathways such as ROCK1—can alter its binding to actin and polyproline ligands, thereby affecting filament assembly and downstream processes like smooth muscle contraction and even immune cell functions. For example, its interaction with cortactin has been linked to the regulation of actin polymerization during contraction events, while in cytotoxic T lymphocytes PFN1 appears to act as a brake on excessive granule release and migration. Such regulatory mechanisms underscore the importance of finely tuning PFN1 activity in both normal physiology and disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "34", "end_ref": "37"}]}, {"type": "t", "text": ""}]}]}]}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Chi-Hong Wu, Claudia Fallini, Nicola Ticozzi, et al. 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