{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n DIPK2B appears to be a member of a family of poorly characterized, kinase‐like proteins associated with the secretory pathway. Recent studies of related kinases have demonstrated that these enzymes localize to the endoplasmic reticulum and Golgi apparatus where they phosphorylate secreted proteins, thereby modulating protein trafficking and extracellular function. In particular, kinases such as Fam20C have been shown to generate the majority of the extracellular phosphoproteome, regulating processes as diverse as biomineralization, lipid homeostasis, wound healing, and cell migration and adhesion (‐"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "‐). Similarly, studies on predicted kinase‐like proteins related to DIPK2B have revealed their localization to the secretory pathway and an ability to influence membrane trafficking via phosphorylation events; proteomic analyses indicate that their substrates often exhibit consensus motifs recognized by proline‐directed and CK2‐type kinases (‐"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": "‐). Moreover, evolutionary and structural analyses of members of this kinase family show conservation of key catalytic and structural motifs – including putative Golgi‐retention sequences and Ca²⁺‐binding domains – that underscore their functional role in regulating secreted protein dynamics (‐"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "‐). Finally, genetic studies implicating related genes in neurodevelopmental disorders, such as autism spectrum disorders and X‐linked mental retardation, support the view that disruption of these secretory pathway kinases can lead to deficits in neuronal development and signaling (‐"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "‐).\n "}]}, {"type": "t", "text": "\n "}, {"type": "p", "children": [{"type": "t", "text": "\n In summary, while DIPK2B remains to be fully explored, evidence from related kinases suggests that it functions as an intracellular phosphotransferase critically involved in the regulation of protein secretion and trafficking. Through its effects on the phosphorylation state of secreted proteins, DIPK2B and its family members likely influence key biological processes ranging from tissue homeostasis and extracellular matrix organization to the regulation of signaling pathways implicated in neurodevelopment and disease.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Vincent S Tagliabracci, Sandra E Wiley, Xiao Guo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A Single Kinase Generates the Majority of the Secreted Phosphoproteome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cell.2015.05.028"}], "href": "https://doi.org/10.1016/j.cell.2015.05.028"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26091039"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26091039"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Agnieszka Hareza, Magda Bakun, Bianka Świderska, et al. 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