The direct binding of the catalytic subunit of protein phosphatase 1 to the PKR protein kinase is necessary but not sufficient for inactivation and disruption of enzyme dimer formation (Q28215791)

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scientific article (publication date: 27 September 2002)

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English	The direct binding of the catalytic subunit of protein phosphatase 1 to the PKR protein kinase is necessary but not sufficient for inactivation and disruption of enzyme dimer formation	scientific article (publication date: 27 September 2002)

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scholarly article

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The direct binding of the catalytic subunit of protein phosphatase 1 to the PKR protein kinase is necessary but not sufficient for inactivation and disruption of enzyme dimer formation (English)

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5

object named as

Michael G Katze

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author name string

Seng-Lai Tan

1

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Semih U Tareen

2

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Mark W Melville

3

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Collin M Blakely

4

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language of work or name

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publication date

27 September 2002

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Journal of Biological Chemistry

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277

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39

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36109-17

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Regulation of translation initiation following stress.

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Translation initiation: adept at adapting

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The emerging role of the interferon-induced PKR protein kinase as an apoptotic effector: a new face of death?

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Double-stranded (ds) RNA binding and not dimerization correlates with the activation of the dsRNA-dependent protein kinase (PKR).

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Characterization of the solution complex between the interferon-induced, double-stranded RNA-activated protein kinase and HIV-I trans-activating region RNA.

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Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI

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Structural requirements for double-stranded RNA binding, dimerization, and activation of the human eIF-2 alpha kinase DAI in Saccharomyces cerevisiae

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Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor

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Mechanism of activation of the double-stranded-RNA-dependent protein kinase, PKR: role of dimerization and cellular localization in the stimulation of PKR phosphorylation of eukaryotic initiation factor-2 (eIF2).

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Characterization of transgenic mice with targeted disruption of the catalytic domain of the double-stranded RNA-dependent protein kinase, PKR.

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Specific phenotypic restoration of an attenuated virus by knockout of a host resistance gene

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Essential role for the dsRNA-dependent protein kinase PKR in innate immunity to viral infection

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Influenza virus NS1 protein counteracts PKR-mediated inhibition of replication.

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The murine double-stranded RNA-dependent protein kinase PKR is required for resistance to vesicular stomatitis virus.

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Detection of protein kinase homologues and viral RNA-binding domains utilizing polyclonal antiserum prepared against a baculovirus-expressed ds RNA-activated 68,000-Da protein kinase

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Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase

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Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase

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The 58-kilodalton inhibitor of the interferon-induced double-stranded RNA-activated protein kinase is a tetratricopeptide repeat protein with oncogenic properties

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Molecular mechanisms responsible for malignant transformation by regulatory and catalytic domain variants of the interferon-induced enzyme RNA-dependent protein kinase

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Mutants of the RNA-dependent protein kinase (PKR) lacking double-stranded RNA binding domain I can act as transdominant inhibitors and induce malignant transformation

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Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR.

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Double-stranded RNA-dependent protein kinase activates transcription factor NF-kappa B by phosphorylating I kappa B.

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Deficient cytokine signaling in mouse embryo fibroblasts with a targeted deletion in the PKR gene: role of IRF-1 and NF-kappaB

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Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways

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Upregulation of STAT1 protein in cells lacking or expressing mutants of the double-stranded RNA-dependent protein kinase PKR.

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Double-stranded-RNA-activated protein kinase PKR enhances transcriptional activation by tumor suppressor p53

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The double-stranded RNA activated protein kinase PKR physically associates with the tumor suppressor p53 protein and phosphorylates human p53 on serine 392 in vitro

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Regulation of double-stranded RNA-activated eukaryotic initiation factor 2α kinase by type 2 protein phosphatase in reticulocyte lysates

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Lambda YES: a multifunctional cDNA expression vector for the isolation of genes by complementation of yeast and Escherichia coli mutations

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Using genetic means to dissect homologous and heterologous protein-protein interactions of PKR, the interferon-induced protein kinase

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Interaction of the interferon-induced PKR protein kinase with inhibitory proteins P58IPK and vaccinia virus K3L is mediated by unique domains: implications for kinase regulation

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Biochemical and genetic evidence for complex formation between the influenza A virus NS1 protein and the interferon-induced PKR protein kinase

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Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein

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Cloning and characterization of a human protein phosphatase 1-encoding cDNA

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The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR

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Functional expression and RNA binding analysis of the interferon-induced, double-stranded RNA-activated, 68,000-Mr protein kinase in a cell-free system

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The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-

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The gamma134.5 protein of herpes simplex virus 1 has the structural and functional attributes of a protein phosphatase 1 regulatory subunit and is present in a high molecular weight complex with the enzyme in infected cells

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The B56alpha regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA-dependent protein kinase PKR

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Specific mutations near the amino terminus of double-stranded RNA-dependent protein kinase (PKR) differentially affect its double-stranded RNA binding and dimerization properties

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Interaction of inhibitor-2 with the catalytic subunit of type 1 protein phosphatase. Identification of a sequence analogous to the consensus type 1 protein phosphatase-binding motif

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The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit

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PACT, a protein activator of the interferon-induced protein kinase, PKR.

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RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling

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Characterization of two evolutionarily conserved, alternatively spliced nuclear phosphoproteins, NFAR-1 and -2, that function in mRNA processing and interact with the double-stranded RNA-dependent protein kinase, PKR

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Phosphorylation of the RNA-dependent protein kinase regulates its RNA-binding activity

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Hepatitis C virus envelope protein E2 does not inhibit PKR by simple competition with autophosphorylation sites in the RNA-binding domain

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Inhibition of myogenesis by depletion of the glycogen-associated regulatory subunit of protein phosphatase-1 in rat skeletal muscle cells

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Expression of a PKR dominant-negative mutant in myogenic cells interferes with the myogenic process

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Stimulation of protein phosphatase activity by insulin and growth factors in 3T3 cells

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Insulin-stimulated phosphorylation of the protein phosphatase-1 striated muscle glycogen-targeting subunit and activation of glycogen synthase

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Identifiers

10.1074/JBC.M205109200

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