{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nWhile the provided abstracts do not explicitly mention SIRPG‐AS1, they describe functions of a related regulatory protein—ASAP2—that may offer context for understanding SIRPG‐AS1’s potential roles. In the first study, ASAP2 is shown to be a critical target during Fcγ receptor–mediated phagocytosis by macrophages. Selenoprotein K (Selk) facilitates the palmitoylation of ASAP2, which in turn permits its cleavage by calpain‐2 within its membrane‐binding BAR domain. This cleavage is necessary for releasing ASAP2 from the phagocytic cup, thereby ensuring the efficient uptake of IgG‐coated targets."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n \nIn a separate investigation, ASAP2 is implicated in the modulation of insulin signaling. Here, ARL15—a protein upregulated by insulin—associates with ASAP2 to enhance the phosphorylation cascade within the canonical insulin receptor pathway. This interaction promotes the pivotal phosphorylation of PDPK1 at Ser241 and subsequently activates AKT, highlighting a role for ASAP2 in maintaining insulin sensitivity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": "\n \nTogether, these studies reveal that ASAP2 serves as a regulatory hub capable of integrating post‐translational modifications with protein–protein interactions to modulate distinct cellular processes. Although SIRPG‐AS1 is not directly addressed in the abstracts, the shared involvement of ASAP2 in key immune and metabolic pathways suggests that if SIRPG‐AS1 is functionally related, it too may influence processes such as phagocytosis and insulin signaling. Further investigation would be required to establish a direct role for SIRPG‐AS1 in these contexts."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Robert L Norton, Gregory J Fredericks, Zhi Huang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Selenoprotein K regulation of palmitoylation and calpain cleavage of ASAP2 is required for efficient FcγR-mediated phagocytosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Leukoc Biol (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1189/jlb.2A0316-156RR"}], "href": "https://doi.org/10.1189/jlb.2A0316-156RR"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27601625"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27601625"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Jie Zhao, Min Wang, Wuquan Deng, et al. "}, {"type": "b", "children": [{"type": "t", "text": "ADP-ribosylation factor-like GTPase 15 enhances insulin-induced AKT phosphorylation in the IR/IRS1/AKT pathway by interacting with ASAP2 and regulating PDPK1 activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2017.03.079"}], "href": "https://doi.org/10.1016/j.bbrc.2017.03.079"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28322786"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28322786"}]}]}]}