{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPalladin is a widely expressed actin‐associated scaffolding protein that organizes and stabilizes the cytoskeleton. By binding directly to major actin‐regulatory proteins – including profilin, alpha‐actinin, VASP, and ezrin – it orchestrates the assembly and maintenance of stress fibers and focal adhesions, thereby influencing cell shape and locomotion. This structural role has been demonstrated in diverse cell types, where palladin recruits actin regulators to specific subcellular sites, ensuring proper actin‐filament dynamics."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn tumor cells, palladin exerts a pivotal role in regulating cell migration and invasion. Through specific phosphorylation events – for example, by Akt1 – palladin modulates F‐actin bundling that is critical for forming specialized structures such as podosomes and invadopodia. These actin‐rich protrusions facilitate extracellular matrix degradation and enable metastatic dissemination in aggressive cancers including breast carcinoma."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPalladin also plays a critical role in stromal cell activation, myofibroblast differentiation, and extracellular matrix remodeling in contexts such as wound healing and cancer-associated desmoplasia. In fibroblasts and adipose-derived stem cells, transforming growth factor–β1 and mechanochemical signals upregulate specific palladin isoforms to promote stress fiber assembly and conversion to a contractile, activated phenotype. Such activation sustains a pro-tumoral microenvironment – as seen in pancreatic ductal adenocarcinoma and other fibrotic tissues – and supports changes in matrix organization that correlate with aggressive tumor behavior."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its structural functions, palladin is integrally regulated by multiple signaling pathways that modify its activity via phosphorylation and protein–protein interactions. For instance, ERK- and Src-mediated phosphorylation modulates its association with other signaling molecules such as Abl, whereas Akt isoforms differentially affect both palladin’s stability and its phosphorylation state. These modifications influence critical processes including spindle orientation, apoptosis (via interaction with ILKAP), and adhesion dynamics in specialized cells like podocytes and mesenchymal tumor cells. Moreover, palladin is engaged in chemomechanically driven fibroblast activation and its altered dynamics have been linked to impaired neurite outgrowth in neural cells."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, extensive clinical and genetic investigations have evaluated palladin’s relevance in human disease. While early studies in familial pancreatic cancer suggested a potential causative mutation in PALLD, subsequent analyses have not substantiated a major role for germline variants. Nonetheless, altered palladin expression – notably within tumor stroma – has been correlated with poor prognosis in malignancies such as renal cell carcinoma and breast cancer, and its genetic variants have been interrogated in the context of coronary heart disease and stroke."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "29", "end_ref": "36"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Malika Boukhelifa, Monica Moza, Thomas Johansson, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Angiotensin II, focal adhesion kinase, and PRX1 enhance smooth muscle expression of lipoma preferred partner and its newly identified binding partner palladin to promote cell migration."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Circ Res (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1161/01.RES.0000261351.54147.de"}], "href": "https://doi.org/10.1161/01.RES.0000261351.54147.de"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17322171"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17322171"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Mikko Rönty, Anu Taivainen, Leena Heiska, et al. 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