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    Prkg2 protein kinase cGMP-dependent 2 [ Rattus norvegicus (Norway rat) ]

    Gene ID: 25523, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Wild-type PKGII phosphorylated Raf-1 at Ser-43 in a cGMP-dependent manner, but a PKGII D412A/R415A mutant, which has a low affinity for cGMP, did not.

    Type II cGMP-dependent protein kinase negatively regulates fibroblast growth factor signaling by phosphorylating Raf-1 at serine 43 in rat chondrosarcoma cells.
    Kamemura N, Murakami S, Komatsu H, Sawanoi M, Miyamoto K, Ishidoh K, Kishimoto K, Tsuji A, Yuasa K.

    06/10/2017
    We conclude that cGKII controls the homeostatic balance of vesicle exocytosis and endocytosis in synaptic boutons of rat cerebellar granule cells.

    The regulation of synaptic vesicle recycling by cGMP-dependent protein kinase type II in cerebellar granule cells under strong and sustained stimulation.
    Collado-Alsina A, Ramírez-Franco J, Sánchez-Prieto J, Torres M., Free PMC Article

    08/23/2014
    Which in turn activates cGKII and induces the phosphorylation of GluA1.

    The type II cGMP dependent protein kinase regulates GluA1 levels at the plasma membrane of developing cerebellar granule cells.
    Incontro S, Ciruela F, Ziff E, Hofmann F, Sánchez-Prieto J, Torres M., Free PMC Article

    09/21/2013
    Sodium depletion enhances renal expression of (pro)renin receptor via cyclic GMP-protein kinase G signaling pathway.

    Sodium depletion enhances renal expression of (pro)renin receptor via cyclic GMP-protein kinase G signaling pathway.
    Huang J, Siragy HM., Free PMC Article

    04/21/2012
    confirmed mutation in Prkg2 is a valuable model for studying dwarfism and longitudinal growth traits

    Phenotypic characterization of the Komeda miniature rat Ishikawa, an animal model of dwarfism caused by a mutation in Prkg2.
    Tsuchida A, Yokoi N, Namae M, Fuse M, Masuyama T, Sasaki M, Kawazu S, Komeda K., Free PMC Article

    01/21/2010
    a subset of phosphorylation sites is modulated, in a cGMP-PKG-specific manner, in intact HEK cells heterologously expressing Cav1.2 alpha(1c) and beta(2a) subunits

    Protein kinase G phosphorylates Cav1.2 alpha1c and beta2 subunits.
    Yang L, Liu G, Zakharov SI, Bellinger AM, Mongillo M, Marx SO.

    01/21/2010
    PKG II activity in zona glomerulosa cells is important for maintaining basal aldosterone production

    cGMP-dependent protein kinase type II regulates basal level of aldosterone production by zona glomerulosa cells without increasing expression of the steroidogenic acute regulatory protein gene.
    Gambaryan S, Butt E, Marcus K, Glazova M, Palmetshofer A, Guillon G, Smolenski A.

    01/21/2010
    results show that the fast phase of autophosphorylation of cGMP dependent protein kinase II has a small effect on its activity, whereas the secondary phase involving Ser126 phosphorylation may generate an active form

    Autophosphorylation of cGMP-dependent protein kinase type II.
    Vaandrager AB, Hogema BM, Edixhoven M, van den Burg CM, Bot AG, Klatt P, Ruth P, Hofmann F, Van Damme J, Vandekerckhove J, de Jonge HR.

    01/21/2010
    Protein kinase G regulation of interleukin 6 promoter signaling pathway largely prevented fluid shear stress-induced increases of IL-6 mRNA in osteosarcoma cells.

    Guanosine 3',5'-cyclic monophosphate (cGMP)/cGMP-dependent protein kinase induce interleukin-6 transcription in osteoblasts.
    Broderick KE, Zhang T, Rangaswami H, Zeng Y, Zhao X, Boss GR, Pilz RB.

    01/21/2010
    eNOS, nNOS, cGMP and protein kinase G mediate the inhibitory effect of pancreastatin on growth and proliferation of hepatoma cells

    eNOS, nNOS, cGMP and protein kinase G mediate the inhibitory effect of pancreastatin, a chromogranin A-derived peptide, on growth and proliferation of hepatoma cells.
    Díaz-Troya S, Najib S, Sánchez-Margalet V.

    01/21/2010
    While nNOS and cGKI mRNA levels steadily increased during development, cGKII mRNA showed a different behaviour pattern, with similar levels observed on postnatal days 7 and 14 and increased levels noted on postnatal day 21.

    Expression of cGMP-dependent protein kinases (I and II) and neuronal nitric oxide synthase in the developing rat cerebellum.
    Jurado S, Sánchez-Prieto J, Torres M.

    01/21/2010
    Inhibition of cGMP-dependent protein kinase II by its own splice isoform

    Inhibition of cGMP-dependent protein kinase II by its own splice isoform.
    Gambaryan S, Palmetshofer A, Glazova M, Smolenski A, Kristjansson GI, Zimmer M, Lohmann SM.

    01/21/2010
    cGMP and cGK II regulate the translocation of CFTR to the apical membrane in rat jejunum

    STa and cGMP stimulate CFTR translocation to the surface of villus enterocytes in rat jejunum and is regulated by protein kinase G.
    Golin-Bisello F, Bradbury N, Ameen N.

    01/21/2010
    Protein kinase G type II activation may define a critical control point for temporal progression into the daytime domain by acting on the positive arm of the transcriptional/translational feedback loop.

    Protein kinase G type II is required for night-to-day progression of the mammalian circadian clock.
    Tischkau SA, Mitchell JW, Pace LA, Barnes JW, Barnes JA, Gillette MU.

    01/21/2010
    the NO-PKG pathway inhibits AGE-induced proliferation by suppressing activation of JAK2-STAT5 and cyclin D1/cdk4 and induction of p21Waf1/Cip1

    Effect of nitric oxide-cGMP-dependent protein kinase activation on advanced glycation end-product-induced proliferation in renal fibroblasts.
    Huang JS, Chuang LY, Guh JY, Chen CJ, Yang YL, Chiang TA, Hung MY, Liao TN.

    01/21/2010
    confirmed that BRIN-BD11 cells (and human islets) express all three known isoforms of PKG (PKG-Ialpha, -Ibeta and II) and provide data suggesting that a transcription-dependent pathway of programmed cell death is involved in the actions of cGMP

    Involvement of the cGMP signalling pathway in the regulation of viability in insulin-secreting BRIN-BD11 cells.
    Kaminski A, Gao H, Morgan NG.

    01/21/2010
    role of cGKII as a molecular switch, coupling the cessation of proliferation and the start of hypertrophic differentiation of chondrocytes through attenuation of Sox9 function

    Cyclic GMP-dependent protein kinase II is a molecular switch from proliferation to hypertrophic differentiation of chondrocytes.
    Chikuda H, Kugimiya F, Hoshi K, Ikeda T, Ogasawara T, Shimoaka T, Kawano H, Kamekura S, Tsuchida A, Yokoi N, Nakamura K, Komeda K, Chung UI, Kawaguchi H., Free PMC Article

    01/21/2010
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