{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSORBS1 encodes the adaptor protein CAP (also known as ponsin), which plays a pivotal role in metabolic signaling. Multiple genetic studies have linked SORBS1 polymorphisms—such as the T228A variant—to improved insulin sensitivity and protection against obesity, type 2 diabetes, hypertension, and even diabetic complications. Consequently, altered SORBS1 expression not only affects insulin‐mediated glucose uptake in adipose and muscle tissues but is also implicated in diverse systemic conditions including endometriosis, ischemic stroke, and vascular dysfunction."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its metabolic functions, SORBS1 is integral to the regulation of cytoskeletal organization and cell adhesion. The CAP/ponsin protein interacts with focal adhesion components and costameric structures to modulate cytoskeletal remodeling during muscle differentiation and regeneration. Studies in both developing and mature muscle cells have revealed that tissue‐specific SORBS1 isoforms contribute to the assembly of cell–matrix contacts, thereby facilitating proper contractile apparatus formation and mechanotransduction in skeletal and cardiac muscle."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMoreover, SORBS1 functions as a tumor suppressor in several cancer types. Reduced SORBS1 expression has been associated with enhanced migratory and invasive cell behavior, in part through activation of JNK/cJun signaling, promotion of epithelial–mesenchymal transition, and interference with p53‐dependent pathways. In breast, bladder, colorectal, and lung cancers the loss or downregulation of SORBS1—as well as its regulation by microRNAs and circular RNAs—correlates with aggressive tumor phenotypes and chemoresistance. Structural studies further underscore that the SH3 domains of CAP/ponsin mediate critical interactions with proteins such as vinculin and components of receptor tyrosine kinase complexes, helping to coordinate adhesion turnover and downstream mitogen‐activated protein kinase signaling. In addition, interactions with nuclear partners expand its regulatory landscape to include aspects of gene transcription and stress responses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Alexandra Nieters, Nikolaus Becker, Jakob Linseisen "}, {"type": "b", "children": [{"type": "t", "text": "Polymorphisms in candidate obesity genes and their interaction with dietary intake of n-6 polyunsaturated fatty acids affect obesity risk in a sub-sample of the EPIC-Heidelberg cohort."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Nutr (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00394-002-0378-y"}], "href": "https://doi.org/10.1007/s00394-002-0378-y"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12395215"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12395215"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "W H Lin, K C Chiu, H M Chang, et al. 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