{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nProtein phosphatase 5 (PPP5C) is a highly conserved serine/threonine phosphatase characterized by an N‐terminal tetratricopeptide repeat (TPR) domain that mediates its autoinhibited state and controls catalytic access. Structural studies have revealed that the TPR domain pivots to block the catalytic groove until activators such as heat shock protein 90, specific lipids (e.g. arachidonic acid) and Ca²⁺/S100 proteins induce conformational changes that relieve autoinhibition. In vitro crystallographic and solution analyses have delineated the precise arrangement of the active site—coordinated by metal ions within conserved motifs—as well as dynamic binding modes with partner peptides, illustrating how PPP5C can be engaged by multiple chaperones to fine‐tune its activity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPPP5C plays a pivotal role in cellular signaling by targeting and dephosphorylating key regulators involved in stress responses and signal transduction. It interacts with proteins in the DNA damage response—dephosphorylating targets such as DNA‐PKcs and 53BP1—to modulate DNA repair and checkpoint activation, and it is essential for proper ATR‐mediated responses. In growth factor signalling, PPP5C attenuates mitogenic cascades by dephosphorylating activating residues on Raf‐1, while it also modulates the circadian clock through regulation of casein kinase Iε activity. Furthermore, PPP5C influences nuclear receptor signalling; estrogen‐induced upregulation of PPP5C leads to dephosphorylation of glucocorticoid receptor residues (e.g. Ser 211), thereby affecting receptor activation and downstream transcriptional responses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "15"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its biochemical regulation, PPP5C exerts profound effects on cell fate and disease. Elevated or dysregulated PPP5C expression has been implicated in various neoplastic settings—including breast cancer, hepatocellular carcinoma, glioma, and bladder cancer—where its function in dephosphorylating cell cycle and stress‐response substrates appears to promote tumor cell proliferation and survival. In cardiomyocytes, PPP5C dephosphorylates the N2B element of titin, thereby modulating myocardial passive tension and kinase signalling. Additional studies highlight its regulation by binding partners such as caveolin‐1 and Rac1, while pharmacological inhibition (as seen with LB‐100) confirms that PPP5C activity can be targeted therapeutically. Finally, transgenic overexpression models have revealed that aberrant PPP5C activity can contribute to tissue hyperplasia, as observed in ocular surface models, further emphasizing its integration into diverse cellular networks."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "26"}]}, {"type": "t", "text": ""}]}]}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Mark R Swingle, Richard E Honkanen, Ewa M Ciszak "}, {"type": "b", "children": [{"type": "t", "text": "Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M402855200"}], "href": "https://doi.org/10.1074/jbc.M402855200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15155720"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15155720"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Jing Yang, S Mark Roe, Matthew J Cliff, et al. 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