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Protein kinase N2

PRK2, protein kinase NII, PKN2
phospholipid-regulated protein kinase, phosphorylates ribosomal protein S6; may play a role in hepatic regulation [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: Rhodopsin, POLYMERASE, PDK1, HAD, V1a
Papers on PRK2
Knockout of the PKN Family of Rho Effector Kinases Reveals a Non-redundant Role for PKN2 in Developmental Mesoderm Expansion.
Cameron et al., Lisbon, Portugal. In Cell Rep, Feb 2016
Here, we describe knockouts of all three mouse PKN isoforms and reveal that PKN2 loss results in lethality at embryonic day 10 (E10), with associated cardiovascular and morphogenetic defects.
CagA of Helicobacter pylori interacts with and inhibits the serine-threonine kinase PRK2.
Stein et al., Albany, United States. In Cell Microbiol, Nov 2015
Here, we describe the effect of CagA on protein kinase C-related kinase 2 (PRK2), which acts downstream of Rho GTPases and is known to affect cytoskeletal rearrangements and cell polarity.
Phosphorylation at the N-terminal finger subdomain of a viral RNA-dependent RNA polymerase.
Villanueva et al., Santiago, Chile. In Biochem Biophys Res Commun, Nov 2015
The RNA-dependent RNA polymerase (RdRP) of the Hepatitis C virus (HCV), named NS5B, is phosphorylated by the cellular protein kinase C-related kinase 2 (PRK2) at two serine residues (Ser29 and Ser42) of the finger subdomain (genotype 1b).
Integrative Genomics-Based Discovery of Novel Regulators of the Innate Antiviral Response.
Huynen et al., Nijmegen, Netherlands. In Plos Comput Biol, Oct 2015
MAP3K11, CDK11B, PSMA3, TRIM14, HSPA9B, CDC37, NUP98, G3BP1), and include uncharacterized factors (DDX17, C6orf58, C16orf57, PKN2, SNW1).
Protein kinase C-related kinase 1 and 2 play an essential role in thromboxane-mediated neoplastic responses in prostate cancer.
Kinsella et al., Dublin, Ireland. In Oncotarget, Oct 2015
PRK1 is a member of a subfamily of three structurally related kinases comprising PRK1/PKNα, PRK2/PKNγ and PRK3/PKNβ that are widely yet differentially implicated in various cancers.
Rho Kinase Pathway Alterations in the Brain and Leukocytes in Huntington's Disease.
Hersch et al., United States. In Mol Neurobiol, Jun 2015
We investigated the messenger RNA (mRNA) expression of Rho kinase pathway genes, including RhoA (Ras homolog family member A), ROCK1 (Rho-associated kinase1), PRK2 (protein kinase C-related protein kinase 2), Profilin1, cofilin1, MYPT1 (myosin phosphatase target subunit 1), and LIMK1 (LIM domain kinase 1) in HD human blood leukocytes, postmortem brain, and in R6/2 HD mouse brain tissue using qPCR.
p38α deficiency and oxidative stress cause cytokinesis failure in hepatocytes.
Sastre et al., Valencia, Spain. In Free Radic Biol Med, 2014
Key proteins of the RhoA pathway (phospho-PRK2, nuclear phosphorylated cofilin, and cytosolic p27) were assessed confirming the impairment of this pathway.
Phosphorylation of hepatitis C virus RNA polymerases ser29 and ser42 by protein kinase C-related kinase 2 regulates viral RNA replication.
Oh et al., Seoul, South Korea. In J Virol, 2014
We previously showed that HCV RdRp is phosphorylated by protein kinase C-related kinase 2 (PRK2).
Constitutively active NDR1-PIF kinase functions independent of MST1 and hMOB1 signalling.
Hergovich et al., London, United Kingdom. In Cell Signal, 2014
Significantly, the analyses of these variants revealed that NDR1-PIF, an NDR1 variant containing the PRK2 hydrophobic motif, remains hyperactive independent of hMOB1/NDR1-PIF complex formation.
Protein Kinase C-Related Kinase (PKN/PRK). Potential Key-Role for PKN1 in Protection of Hypoxic Neurons.
Baier-Bitterlich et al., Innsbruck, Austria. In Curr Neuropharmacol, 2014
Serine/threonine protein kinase C-related kinase (PKN/PRK) is a family of three isoenzymes (PKN1, PKN2, PKN3), which are widely distributed in eukaryotic organisms and share the same overall domain structure.
Enzyme Kinetics and Distinct Modulation of the Protein Kinase N Family of Kinases by Lipid Activators and Small Molecule Inhibitors.
Timofeevski et al., In Biosci Rep, 2014
The known lipid effector, arachidonic acid, increased the catalytic efficiency of each isoform, mainly through an increase in kcat for PKN1 and PKN2, and a decrease in peptide KM for PKN3.
Manipulation of pro-inflammatory cytokine production by the bacterial cell-penetrating effector protein YopM is independent of its interaction with host cell kinases RSK1 and PRK2.
Rüter et al., Münster, Germany. In Virulence, 2013
The C-terminus of rYopM was identified to be essential for the interaction with RSK1, whereas any deletion in rYopM's leucin-rich repeat domains abrogated PRK2 binding.
Regulation of protein kinase C-related protein kinase 2 (PRK2) by an intermolecular PRK2-PRK2 interaction mediated by Its N-terminal domain.
Neimanis et al., Frankfurt am Main, Germany. In J Biol Chem, 2012
Regulation of protein kinase C-related protein kinase 2 (PRK2) by an intermolecular PRK2-PRK2 interaction mediated by Its N-terminal domain.
Destabilization of PDK1 by Hsp90 inactivation suppresses hepatitis C virus replication through inhibition of PRK2-mediated viral RNA polymerase phosphorylation.
Oh et al., Seoul, South Korea. In Biochem Biophys Res Commun, 2012
these findings suggest that Hsp90 plays a critical role in the regulation of HCV RNA polymerase phosphorylation via the PDK1-PRK2 signaling pathway.
The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells.
Hall et al., New York City, United States. In Mol Cell Biol, 2011
Rho binding is essential for PRK2 function and facilitates PRK2 recruitment to junctions. Kinase-dead PRK2 acts as a dominant-negative mutant and prevents apical junction formation.
Regulatory domain selectivity in the cell-type specific PKN-dependence of cell migration.
Parker et al., London, United Kingdom. In Plos One, 2010
PKN isoforms are not simply redundant in supporting migration, but appear to be linked through isoform specific regulatory domain properties to selective upstream signals. It
Delineation of regions of the Yersinia YopM protein required for interaction with the RSK1 and PRK2 host kinases and their requirement for interleukin-10 production and virulence.
Bliska et al., Stony Brook, United States. In Infect Immun, 2010
Yersinia pseudotuberculosis mutants expressing YopM proteins unable to interact with either RSK1 or PRK2 were defective for virulence in this assay, indicating that both interaction domains are important for YopM to promote pathogenesis.
Nonstructural protein 5B of hepatitis C virus.
Myung et al., South Korea. In Mol Cells, 2006
Cellular proteins interacting with NS5B include VAMP-associated proteins, heIF4AII, hPLIC1, nucleolin, PRK2, a-actinin, and p68 helicase.
The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC.
Mukai, Kōbe, Japan. In J Biochem, 2003
There are at least three different isoforms of PKN (PKNalpha/PAK-1/PRK-1, PKNbeta, and PRK2/PAK-2/PKNgamma) in mammals, each of which shows different enzymological properties, tissue distribution, and varied functions.
[The participation of transmembrane messenger systems in the action of steroid hormones on target cells].
Sidorkina et al., In Fiziol Zh Sssr Im I M Sechenova, 1990
Estradiol causes protein kinases A translocation into the cell nuclei and enhances the protein kinase NII activity.
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