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    Tpcn1 two pore channel 1 [ Mus musculus (house mouse) ]

    Gene ID: 252972, updated on 19-Sep-2021

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Genetic Inactivation of Two-Pore Channel 1 Impairs Spatial Learning and Memory.

    Genetic Inactivation of Two-Pore Channel 1 Impairs Spatial Learning and Memory.
    Mallmann RT, Klugbauer N., Free PMC Article

    TPC1 directly interacts with syntaxins and regulates protein processing through early and recycling endosomes.

    The two-pore channel TPC1 is required for efficient protein processing through early and recycling endosomes.
    Castonguay J, Orth JHC, Müller T, Sleman F, Grimm C, Wahl-Schott C, Biel M, Mallmann RT, Bildl W, Schulte U, Klugbauer N., Free PMC Article

    electron cryo-microscopy structures of mouse TPC1 (MmTPC1)-a voltage-dependent, phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2)-activated Na(+)-selective channel-in both the apo closed state and ligand-bound open state

    Structural insights into the voltage and phospholipid activation of the mammalian TPC1 channel.
    She J, Guo J, Chen Q, Zeng W, Jiang Y, Bai XC., Free PMC Article

    TPC1 and TPC2 were found to be essential for appropriate basal and induced autophagic flux in cardiomyocytes.

    Endolysosomal two-pore channels regulate autophagy in cardiomyocytes.
    García-Rúa V, Feijóo-Bandín S, Rodríguez-Penas D, Mosquera-Leal A, Abu-Assi E, Beiras A, María Seoane L, Lear P, Parrington J, Portolés M, Roselló-Lletí E, Rivera M, Gualillo O, Parra V, Hill JA, Rothermel B, González-Juanatey JR, Lago F., Free PMC Article

    The results confirmed the altered expression of HFABP, a key fatty acid transport protein, and of enolase and PGK1, the key enzymes in the glycolytic process

    Metabolic alterations derived from absence of Two-Pore Channel 1 at cardiac level.
    Garcia-Rua V, Feijoo-Bandin S, Garcia-Vence M, Aragon-Herrera A, Bravo SB, Rodriguez-Penas D, Mosquera-Leal A, Lear PV, Parrington J, Alonso J, Rosello-Lleti E, Portoles M, Rivera M, Gonzalez-Juanatey JR, Lago F.

    Mice lacking the endo-lysosomal TPC1 were protected from myocardial ischemia reperfusion injury.

    Inhibition of NAADP signalling on reperfusion protects the heart by preventing lethal calcium oscillations via two-pore channel 1 and opening of the mitochondrial permeability transition pore.
    Davidson SM, Foote K, Kunuthur S, Gosain R, Tan N, Tyser R, Zhao YJ, Graeff R, Ganesan A, Duchen MR, Patel S, Yellon DM., Free PMC Article

    Genetic ablation of endolysosomal TPC1 or TPC2 channels attenuates glucose- and sulfonylurea-induced membrane currents, depolarization, cytoplasmic Ca2+ signals, and insulin secretion in pancreatic beta cells.

    Nicotinic Acid Adenine Dinucleotide Phosphate (NAADP) and Endolysosomal Two-pore Channels Modulate Membrane Excitability and Stimulus-Secretion Coupling in Mouse Pancreatic β Cells.
    Arredouani A, Ruas M, Collins SC, Parkesh R, Clough F, Pillinger T, Coltart G, Rietdorf K, Royle A, Johnson P, Braun M, Zhang Q, Sones W, Shimomura K, Morgan AJ, Lewis AM, Chuang KT, Tunn R, Gadea J, Teboul L, Heister PM, Tynan PW, Bellomo EA, Rutter GA, Rorsman P, Churchill GC, Parrington J, Galione A., Free PMC Article

    It was concluded that Tpcn1/2(-/-) mice show mature-onset obesity due to reduced lipid availability and use, and a defect in beta-adrenergic receptor signaling, leading to impaired thermogenic activity, in brown adipose tissue.

    Absence of intracellular ion channels TPC1 and TPC2 leads to mature-onset obesity in male mice, due to impaired lipid availability for thermogenesis in brown adipose tissue.
    Lear PV, González-Touceda D, Porteiro Couto B, Viaño P, Guymer V, Remzova E, Tunn R, Chalasani A, García-Caballero T, Hargreaves IP, Tynan PW, Christian HC, Nogueiras R, Parrington J, Diéguez C., Free PMC Article

    Results report the existence of a novel, alternative variant isoform of Tpcn1, termed Tpcn1B, resulting from an alternative promoter and giving rise to a TPC1B protein with an N-terminal truncation relative to the sequence of the TPC1A.

    TPC1 has two variant isoforms, and their removal has different effects on endo-lysosomal functions compared to loss of TPC2.
    Ruas M, Chuang KT, Davis LC, Al-Douri A, Tynan PW, Tunn R, Teboul L, Galione A, Parrington J., Free PMC Article

    NAADP and the two-pore calcium channel TPC1 participate in the acrosome reaction in mammalian spermatozoa.

    NAADP and the two-pore channel protein 1 participate in the acrosome reaction in mammalian spermatozoa.
    Arndt L, Castonguay J, Arlt E, Meyer D, Hassan S, Borth H, Zierler S, Wennemuth G, Breit A, Biel M, Wahl-Schott C, Gudermann T, Klugbauer N, Boekhoff I., Free PMC Article

    TPC1 is a member of a new family of voltage-gated Na(+) channels that senses pH changes and confers electrical excitability to organelles.

    The voltage-gated sodium channel TPC1 confers endolysosomal excitability.
    Cang C, Bekele B, Ren D.

    We find alterations in two-pore calcium channel protein expression, with loss of presenilin preventing the formation of a high molecular weight species of TPC1 and TPC2.

    Presenilin-null cells have altered two-pore calcium channel expression and lysosomal calcium: implications for lysosomal function.
    Neely Kayala KM, Dickinson GD, Minassian A, Walls KC, Green KN, Laferla FM., Free PMC Article

    Study identifies an endolysosomal ATP-sensitive Na channel - a complex formed by two-pore channels TPC1 and TPC2; channel complex detects nutrient status, becomes constitutively open upon nutrient removal and mTOR translocation off the lysosomal membrane, and controls the lysosome's membrane potential, pH stability, and amino acid homeostasis.

    mTOR regulates lysosomal ATP-sensitive two-pore Na(+) channels to adapt to metabolic state.
    Cang C, Zhou Y, Navarro B, Seo YJ, Aranda K, Shi L, Battaglia-Hsu S, Nissim I, Clapham DE, Ren D., Free PMC Article

    Study finds by direct patch-clamp analysis of endolysosomal membranes that PI(3,5)P2 specifically activates TPCs and, unexpectedly, that nicotinic acid adenine dinucleotide phosphate does not. TPC1 and TPC2-mediated currents are selective for Na+, which is the predominant cation in the lysosome.

    TPC proteins are phosphoinositide- activated sodium-selective ion channels in endosomes and lysosomes.
    Wang X, Zhang X, Dong XP, Samie M, Li X, Cheng X, Goschka A, Shen D, Zhou Y, Harlow J, Zhu MX, Clapham DE, Ren D, Xu H., Free PMC Article

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