{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRecent proteomics analyses of protocadherin‐γ complexes in the vertebrate central nervous system revealed a broad repertoire of associated proteins—over 120 candidates besides the core clustered protocadherins—that are thought to contribute to the integrity and function of the postsynaptic density. Although the specific biological role of ANKRD20A5P is not explicitly defined in these studies, its identification among the non‐redundant proteins associated with protocadherin complexes suggests that it may be involved in maintaining the structural stability or modulating the activity of protein assemblies critical for synaptic development and neuronal survival."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn a related investigation examining the regulatory mechanisms of CaMKP activity, the processed C-terminal fragment of a protocadherin‑γ member was shown to function as a scaffold to promote dephosphorylation of CaMKI, implicating a role for protocadherin‐dependent modulation of intracellular calcium signaling pathways. By analogy, although direct functional data for ANKRD20A5P are not provided, its presence within these protein complexes raises the possibility that it could participate in, or modulate, such signaling networks—thereby contributing to the fine regulation of kinase/phosphatase activity that is essential for proper neural function."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Meng-Hsuan Han, Chengyi Lin, Shuxia Meng, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Proteomics analysis reveals overlapping functions of clustered protocadherins."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Proteomics (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/mcp.M900343-MCP200"}], "href": "https://doi.org/10.1074/mcp.M900343-MCP200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19843561"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19843561"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Takashi Onouchi, Yoshimi Kishino-Kaneko, Isamu Kameshita, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Regulation of Ca(2+)/calmodulin-dependent protein kinase phosphatase (CaMKP/PPM1F) by protocadherin-γC5 (Pcdh-γC5)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Arch Biochem Biophys (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.abb.2015.09.014"}], "href": "https://doi.org/10.1016/j.abb.2015.09.014"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26386307"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26386307"}]}]}]}