{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nThe scientific studies provided largely focus on the multifunctional protein EPLIN (also known as LIMA1) and its central role in regulating cell adhesion and the actin cytoskeleton. For example, EPLIN couples with the cadherin–catenin complex to stabilize F‐actin within the adhesion belt of epithelial cells, thereby ensuring robust cell–cell adhesion (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " In addition, EPLIN is implicated in intestinal cholesterol absorption by bridging key proteins such as NPC1L1 to a transport complex, thereby regulating lipid uptake (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nOther studies have revealed that EPLIN’s function is dynamically regulated by signaling pathways. For instance, ERK-dependent phosphorylation of EPLIN reduces its affinity for actin filaments, facilitating the reorganization of the cytoskeleton that underlies enhanced cell motility and wound healing (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": " Furthermore, EPLIN’s proper localization to actin structures is critical for its role in suppressing oncogenic transformation, as demonstrated in cellular models in which its enforced expression counteracts transformation by certain oncogenes (see"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": ", and its association with integrin adhesion complexes via PINCH-1 supports effective adhesion and migration processes (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAt the transcriptional level, EPLIN expression is regulated by actin–MAL–SRF signaling, linking the state of the cytoskeleton to its tumor suppressor functions (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": " Moreover, EPLIN plays roles in developmental contexts by controlling membrane dynamics and mitochondrial energetics in pluripotent stem cells, thereby influencing cellular integration during early embryogenesis (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": " A final study, although focused on extracellular vesicle-mediated communication in liver fibrosis, does not report any function related to EPLIN or SNORA17B (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIt is important to note that none of these abstracts describe or characterize a function for SNORA17B. Instead, they consistently address the diverse roles of EPLIN/LIMA1 in cell–cell adhesion, cytoskeletal regulation, motility, transformation suppression, and developmental processes. Thus, while these studies provide significant insights into EPLIN biology, they do not offer any information regarding the function of SNORA17B. Future investigations would be required to determine whether SNORA17B plays any role in these or other related cellular pathways.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Kentaro Abe, Masatoshi Takeichi "}, {"type": "b", "children": [{"type": "t", "text": "EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0710504105"}], "href": "https://doi.org/10.1073/pnas.0710504105"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18093941"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18093941"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Ying-Yu Zhang, Zhen-Yan Fu, Jian Wei, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A "}, {"type": "a", "children": [{"type": "t", "text": "i"}], "href": "i"}, {"type": "t", "text": "LIMA1"}, {"type": "a", "children": [{"type": "t", "text": "/i"}], "href": "/i"}, {"type": "t", "text": " variant promotes low plasma LDL cholesterol and decreases intestinal cholesterol absorption."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Science (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/science.aao6575"}], "href": "https://doi.org/10.1126/science.aao6575"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29880681"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29880681"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Mei-Ying Han, Hidetaka Kosako, Toshiki Watanabe, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Inhibition of anchorage-independent growth of transformed NIH3T3 cells by epithelial protein lost in neoplasm (EPLIN) requires localization of EPLIN to actin cytoskeleton."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Biol Cell (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1091/mbc.01-08-0414"}], "href": "https://doi.org/10.1091/mbc.01-08-0414"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11950948"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11950948"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Esra Karaköse, Tamar Geiger, Kevin Flynn, et al. 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