{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n Recent studies indicate that proteins harboring the DALIR module function as multifaceted molecular adaptors that integrate and modulate a variety of cellular signals by orchestrating specific protein–protein interactions. In several systems, these proteins contribute to the spatial organization of signaling complexes, ensuring that receptor–ligand engagements or post‐translational modifications are tightly coupled to downstream responses. For example, in immune cells the segregation of kinases and regulatory phosphatases at sites of close contact enhances receptor triggering, thereby amplifying T cell activation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " Similarly, members of this protein class contribute to innate tumor surveillance by mediating noncanonical receptor–ligand interactions that drive cytolytic responses in natural killer cells."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In other contexts, the DALIR-containing proteins act as regulatory scaffolds that couple extracellular or stress‐related cues with gene expression control. Phosphorylation‐induced conformational changes in such regulators can modulate mRNA decay pathways and influence nuclear localization, thereby linking signaling events to transcript turnover."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": " Furthermore, specialized domains—including RING and zinc–binding motifs—embedded within these proteins instigate ubiquitination events that fine‐tune the stability and assembly of multiprotein complexes, a function critical for pathways such as Notch and WNT signaling."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": " \n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Collectively, the DALIR module appears to serve as a conserved platform that not only stabilizes the structural integrity of large protein assemblies but also regulates the dynamic interplay between signal reception and effector responses. This integrative role is essential for maintaining cellular homeostasis and enabling rapid, context–dependent adaptations to both extracellular ligands and intracellular stress signals.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Veronica T Chang, Ricardo A Fernandes, Kristina A Ganzinger, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Struct Mol Biol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nsmb.1558"}], "href": "https://doi.org/10.1038/nsmb.1558"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19198587"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19198587"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Digant Nayak, J Sivaraman "}, {"type": "b", "children": [{"type": "t", "text": "Structural basis for the indispensable role of a unique zinc finger motif in LNX2 ubiquitination."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncotarget (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/oncotarget.5326"}], "href": "https://doi.org/10.18632/oncotarget.5326"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26451611"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26451611"}]}]}]}