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drug target
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CTP:phosphocholine cytidylyltransferase beta3 (CCTbeta3) may be targeted to suppress prolonged autophagy in cancer cells in vivo
evolution
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the enzyme is a member of the cytidylyltransferase family of enzymes that utilize cytidine 5'-triphosphate (CTP) to synthesize molecules that are typically precursors to membrane phospholipids
evolution
the conformational malleability of the x02E helix pair that bridges the membrane binding and catalytic domains of the enzyme makes it an ideal element adapted by evolution for transducing signals from membrane to active site
malfunction
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acute prelamin A accumulation after reduction of the activity of the ZMPSTE24 endoprotease by siRNA knockdown, results in the generation of a complex nucleoplasmic reticulum that depends for its formation on the CTP:phosphocholinecytidylyltransferase-a, this structure can form during interphase, confirming that it is independent of mitosis and therefore not a consequence of disordered nuclear envelope assembly
malfunction
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isozyme CTbeta2 deficiency in distal axons reduces the incorporation of choline into by 95% whereas phosphatidylcholine synthesis in cell bodies/proximal axons is unaltered. Brains of mice lacking CTbeta2 have normal phosphatidylethanolamine content despite having 35% lower enzyme activity than wild-type brains. Axon branching, but not axon extension, is impaired in CTbeta2-deficient neurons. Phenotypes, overview
malfunction
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isozyme CTbeta2 deficiency in distal axons reduces the incorporation of choline into by 95% whereas phosphatidylcholine synthesis in cell bodies/proximal axons is unaltered. Brains of mice lacking CTbeta2 have normal phosphatidylethanolamine content despite having 35% lower enzyme activity than wild-type brains. Axon branching, but not axon extension, is impaired in CTbeta2-deficient neurons. Phenotypes, overview
malfunction
mutations in the gene encoding CTP:phosphocholine cytidylyltransferase (PCYT1A) cause three distinct pathologies in humans: lipodystrophy, spondylometaphyseal dysplasia with cone-rod dystrophy (SMD-CRD), and isolated retinal dystrophy
malfunction
without cholinephosphate cytidylyltransferase (CPCT), Leishmania major parasites cannot incorporate choline into phosphatidylcholine, yet the CPCT-null mutants contain similar levels of phosphatidylcholine and phosphatidylethanolamine as wild type parasites. Loss of CPCT does not affect the growth of parasites in complete medium or their virulence in mice. The results suggest that other mechanisms of phosphatidylcholine synthesis can compensate the loss of CPCT. CPCT-null parasites exhibit severe growth defects when ethanolamine and exogenous lipids became limited or when they are co-cultured with certain bacteria that are known to be members of sandfly midgut microbiota
malfunction
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isozyme CTbeta2 deficiency in distal axons reduces the incorporation of choline into by 95% whereas phosphatidylcholine synthesis in cell bodies/proximal axons is unaltered. Brains of mice lacking CTbeta2 have normal phosphatidylethanolamine content despite having 35% lower enzyme activity than wild-type brains. Axon branching, but not axon extension, is impaired in CTbeta2-deficient neurons. Phenotypes, overview
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metabolism
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the enzyme catalyzes a step in the Kennedy pathway for phosphatidylecholine synthesis, overview
metabolism
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the enzyme catalyzes a step in the Kennedy pathway for phosphatidylecholine synthesis, overview
metabolism
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the enzyme catalyzes conversion of phosphocholine and CTP to cytidine diphosphocholine (CDP-choline), a step critical for synthesis of the membrane phospholipid phosphatidylcholine
metabolism
CTP:phosphocholine cytidylyltransferase is the key regulatory enzyme in phosphatidylcholine synthesis
metabolism
key enzyme in phosphatidylcholine synthesis
metabolism
rate limiting step of the de novo phosphatidylcholine biosynthesis is catalysed by CTP:phosphocholine cytidylyltransferase, which has a key regulatory function within the pathway
metabolism
rate-limiting enzyme of the lipid biosynthesis pathway
metabolism
the enzyme catalyzes the formation of CDP-choline, a key intermediate in the choline branch of the Kennedy pathway
physiological function
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CTP:phosphocholine cytidylyltransferase alpha is a nuclear enzyme that catalyzes the rate-limiting step in the CDP-choline pathway for phosphatidylcholine synthesis. Lipid activation of the enzyme results in its translocation to the nuclear envelope and expansion of an intranuclear membrane network termed the nucleoplasmic reticulum by a mechanism involving membrane deformation. CCTalpha and lamins specifically cooperate to form the nucleoplasmic reticulum, but the overall structure of the nuclear envelope has a minimal impact on enzyme activity and phosphocholine synthesis
physiological function
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CTP:phosphocholine cytidylyltransferase alpha is a nuclear enzyme that catalyzes the rate-limiting step in the CDP-choline pathway for phosphatidylcholine synthesis. The enzyme is not involved in the Hutchinson-Gilford progeria syndrome, overview
physiological function
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CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis
physiological function
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CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis
physiological function
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CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis
physiological function
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CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis
physiological function
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importance of isozyme CTbeta2 for phosphatidylcholine synthesis as well as for axon formation, growth and branching of primary sympathetic neurons
physiological function
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importance of isozyme CTbeta2 for phosphatidylcholine synthesis as well as for axon formation, growth and branching of primary sympathetic neurons
physiological function
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nucleoplasmic reticulum development seems dependent on the enzyme CTP:phosphocholine-cytidylyltransferase-alpha, which is responsible for phosphatidylcholine synthesis for the biosynthesis and curvature of membranes, but nucleoplasmic reticulum development is independent of mitosis. Colocalisation of prelamin A and lamin B1 with a developing nucleoplasmic reticulum is dependent on CTP:phosphocholine-cytidylyltransferase-alpha
physiological function
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phosphatidylcholine acts as a surfactant to prevent lipid droplet coalescence, which otherwise yields large, lipolysis-resistant lipid droplets and triglyceride accumulation. The need for additional phosphatidylecholine to coat the enlarging surface during lipid droplet expansion is provided by the Kennedy pathway, which is activated by reversible targeting of the rate-limiting enzyme, CTP:phosphocholine cytidylyltransferase, to growing lipid droplet surfaces. CCT1 regulates lipid droplet size and triacylgylceride storage in vivo
physiological function
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phosphatidylcholine acts as a surfactant to prevent lipid droplet coalescence, which otherwise yields large, lipolysis-resistant lipid droplets and triglyceride accumulation. The need for additional phosphatidylecholine to coat the enlarging surface during lipid droplet expansion is provided by the Kennedy pathway, which is activated by reversible targeting of the rate-limiting enzyme, CTP:phosphocholine cytidylyltransferase, to growing lipid droplet surfaces. CCT1 regulates lipid droplet size and triacylgylceride storage in vivo
physiological function
CTP:phosphocholine cytidylyltransferase-alpha (CCTalpha) and CCTbeta catalyze the rate limiting step in phosphatidylcholine biosynthesis
physiological function
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key regulatory enzyme for phosphatidylcholine synthesis in plants
physiological function
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phosphatidylcholine synthesis through CCTbeta3 (CTP:phosphocholine cytidylyltransferase beta3) activation on lipid droplets is crucial for sustaining autophagy and long-term cell survival
physiological function
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importance of isozyme CTbeta2 for phosphatidylcholine synthesis as well as for axon formation, growth and branching of primary sympathetic neurons
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additional information
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the enzyme is composed of a catalytic head domain and a regulatory tail, the latter is composed of a long membrane lipid-inducible amphipathic helix, followed by a highly disordered segment. The tail region has dual functions as a regulator of membrane binding/enzyme activation and as an inhibitor of catalysis in the unbound form of the enzyme, suggesting conformational plasticity. Full activation of CCTmay require not only loss of a silencing conformation in the membrane-inducible amphipathic helix but a gain of an activating conformation, promoted by membrane binding
additional information
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the enzyme is composed of a catalytic head domain and a regulatory tail, the latter is composed of a long membrane lipid-inducible amphipathic helix, followed by a highly disordered segment. The tail region has dual functions as a regulator of membrane binding/enzyme activation and as an inhibitor of catalysis in the unbound form of the enzyme, suggesting conformational plasticity. Full activation of CCTmay require not only loss of a silencing conformation in the membrane-inducible amphipathic helix but a gain of an activating conformation, promoted by membrane binding. The conserved 22-residue segment in domain M contributes to both silencing and membrane binding/activation of metazoan
additional information
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the enzyme is composed of a catalytic head domain and a regulatory tail, the latter is composed of a long membrane lipid-inducible amphipathic helix, followed by a highly disordered segment. The tail region has dual functions as a regulator of membrane binding/enzyme activation and as an inhibitor of catalysis in the unbound form of the enzyme, suggesting conformational plasticity. Full activation of CCTmay require not only loss of a silencing conformation in the membrane-inducible amphipathic helix but a gain of an activating conformation, promoted by membrane binding. The conserved 22-residue segment in domain M contributes to both silencing and membrane binding/activation of metazoan
additional information
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the enzyme is composed of a catalytic head domain and a regulatory tail, the latter is composed of a long membrane lipid-inducible amphipathic helix, followed by a highly disordered segment. The tail region has dual functions as a regulator of membrane binding/enzyme activation and as an inhibitor of catalysis in the unbound form of the enzyme, suggesting conformational plasticity. Full activation of CCTmay require not only loss of a silencing conformation in the membrane-inducible amphipathic helix but a gain of an activating conformation, promoted by membrane binding. The conserved 22-residue segment in domain M contributes to both silencing and membrane binding/activation of metazoan