{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n Recent proteomic and functional studies have established that actin beta‐like protein 2 (ACTBL2) is a novel member of the actin isoform family that plays multifaceted roles in cancer and cellular motility. In colorectal cancer, for instance, ACTBL2 was found to be upregulated in tumor tissues compared with adjacent normal mucosa, supporting its emerging role as a novel disease‐associated biomarker."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " In parallel, work in human melanoma cells demonstrated that ACTBL2 directly interacts with cytoskeletal regulators such as gelsolin, suggesting that it may participate in the remodeling of the actin network and thereby influence cell dynamics."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " Moreover, investigations in breast cancer have identified that ACTBL2 competes for binding to MTSS1, a metastasis suppressor, with RBCK1; this competition modulates NF‐κB signaling and thereby promotes the maintenance of tumor‐initiating cells."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In ovarian cancer, several independent studies have reported deregulated ACTBL2 expression as part of gene signatures linked to disease progression, chemoresistance, and worse patient survival."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "7"}]}, {"type": "t", "text": " Similar oncogenic potential has been implied in thymoma, where network analyses nominate ACTBL2 among potential therapeutic targets"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": ", and even in studies addressing genomic alterations in syndromes related to DNA repair deficiencies."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Complementary chemical proteomics approaches have identified ACTBL2 as a binding partner for bioactive compounds with anti‐tumor properties."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": " Furthermore, reviews of actin isoform biology have emphasized that ACTBL2, as a putative “seventh” actin, exhibits distinct amino acid substitutions and supports key processes such as focal adhesion formation, actin polymerization, and the formation of lamellipodia and stress fibers, all of which are crucial for regulating cell motility."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In summary, the current body of evidence indicates that ACTBL2 is not merely a structural component of the actin cytoskeleton but also a dynamic regulator of signal transduction and cellular behavior in various malignancies. Its aberrant expression and interactions with other cytoskeletal and signaling molecules underscore its potential utility as a diagnostic biomarker and therapeutic target in cancer.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Saba Ghazanfar, Iram Fatima, Muhammad Aslam, et al. 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