{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nAlthough none of the provided abstracts mention MIR4264 directly, the studies collectively describe a network of adaptor proteins that finely tune Src family kinase (SFK) signaling. In one study"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": ", the adaptor protein Tom1L1 was identified as both a substrate and an activator of SFKs. Intriguingly, Tom1L1 does not enhance DNA synthesis despite stimulating Src activity; rather, it negatively regulates PDGF-induced mitogenic signaling by altering the association of SFKs with their receptors. This observation suggests that factors modulating similar adaptors could potentially influence the broader SFK signaling cascade, raising the possibility that MIR4264 might regulate the expression or activity of components such as Tom1L1, thereby indirectly affecting cell proliferation signals.\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn a second study"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": ", the SFK regulator Srcasm was shown to act as a molecular “rheostat” in epithelial cells. Srcasm promotes the down-regulation of the active Fyn kinase through a phosphorylation-dependent mechanism, which in turn modulates epidermal growth and differentiation. Given that precise control of kinase activity is essential for maintaining cellular homeostasis, one could speculate that MIR4264 might play a role in fine-tuning such regulatory nodes by targeting transcripts encoding proteins like Srcasm or its interacting partners.\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nA third study"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "further demonstrated that the formation of a complex between Tom1L1 and clathrin heavy chain (CHC) governs the subcellular partitioning of SFKs and thereby limits their interaction with the PDGF receptor—a critical step for mitogenic signaling and transformation. The ability to modulate the spatial distribution of SFK activity is central to controlling mitogenesis. In this context, MIR4264 may be envisaged as a post‐transcriptional regulator whose expression could influence the levels of these adaptor proteins and complexes, ultimately impacting the membrane microdomain organization and the strength of SFK-driven mitogenic pathways.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Mélanie Franco, Olivia Furstoss, Valérie Simon, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The adaptor protein Tom1L1 is a negative regulator of Src mitogenic signaling induced by growth factors."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.26.5.1932-1947.2006"}], "href": "https://doi.org/10.1128/MCB.26.5.1932-1947.2006"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16479011"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16479011"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Weijie Li, Christine Marshall, Lijuan Mei, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Srcasm corrects Fyn-induced epidermal hyperplasia by kinase down-regulation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M606583200"}], "href": "https://doi.org/10.1074/jbc.M606583200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17046829"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17046829"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Guillaume Collin, Mélanie Franco, Valérie Simon, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The Tom1L1-clathrin heavy chain complex regulates membrane partitioning of the tyrosine kinase Src required for mitogenic and transforming activities."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.00543-07"}], "href": "https://doi.org/10.1128/MCB.00543-07"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17785434"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17785434"}]}]}]}