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Steady-state kinetic analysis revealed that PKN1 (show PKN1 Proteins)-3 follows a sequential ordered Bi-Bi (show CACNA1A Proteins) kinetic mechanism, where peptide substrate binding is preceded by ATP binding. This kinetic mechanism was confirmed by additional kinetic studies for product inhibition and affinity of small molecule inhibitors.
PKN2 knockdown in vitro decreased insulin-stimulated glucose uptake, incorporation into glyco (show PRKAA1 Proteins)gen, and oxidation. Thus, PKN2 alters key signaling pathways and transcriptional networks to regulate glucose and lipid metabolism.
Helicobacter pylori CagA (show S100A8 Proteins) interacts with PRK2 and inhibits its kinase activity.
TXA2 (show TBXA2R Proteins)-mediated neoplastic responses in prostate adenocarcinoma PC-3 (show PCSK1 Proteins) cells occur through a PRK1 (show PKN1 Proteins)/PRK2-dependent mechanism.
findings demonstrate that Yersinia enterocolitica rYopM interacts with RSK1 (show RPS6KA1 Proteins) and PRK2 following cell-penetration
Regulation of protein kinase C-related (show PKN1 Proteins) protein kinase 2 (PRK2) by an intermolecular PRK2-PRK2 interaction mediated by Its N-terminal domain.
these findings suggest that Hsp90 (show HSP90 Proteins) plays a critical role in the regulation of HCV RNA polymerase phosphorylation via the PDK1 (show PDK1 Proteins)-PRK2 signaling pathway.
PKN (show PKN1 Proteins) isoforms are not simply redundant in supporting migration, but appear to be linked through isoform specific regulatory domain properties to selective upstream signals. It
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.
Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases.
In mature skeletal muscle, in vivo PKN2 knockdown decreased glucose uptake and increased AMPK (show PRKAA1 Proteins) phosphorylation. Thus, PKN2 alters key signaling pathways and transcriptional networks to regulate glucose and lipid metabolism.
Mechanistically, Yersinia pseudotuberculosis YopM recruits and activates the mouse host kinases PRK1 (show PKN1 Proteins) and PRK2 to negatively regulate pyrin (show MEFV Proteins) by phosphorylation.
PKN2 formed complexes with Cdo (show CDO1 Proteins), APPL1 (show APPL1 Proteins) and AKT (show AKT1 Proteins) via its C-terminal region and this interaction appeared to be important for induction of AKT (show AKT1 Proteins) activity as well as myoblast differentiation.
To unravel the in vivo physiological function of PKN2, we targeted the PKN2 gene. Constitutive disruption of the mouse PKN2 gene resulted in growth retardation and lethality before embryonic day (E) 10.5. PKN2(-/-) embryo did not undergo axial turning and showed insufficient closure of the neural tube.Mouse embryonic fibroblasts (MEFs) derived from PKN2(-/-) embryos at E9.5 failed to grow.
Yersinia pseudotuberculosis mutants expressing YopM proteins unable to interact with either RSK1 (show RPS6KA1 Proteins) or PRK2 were defective for virulence in this assay, indicating that both interaction domains are important for YopM to promote pathogenesis.
phospholipid-regulated protein kinase, phosphorylates ribosomal protein S6\; may play a role in hepatic regulation
, cardiolipin-activated protein kinase Pak2
, protein kinase C-like 2
, protein-kinase C-related kinase 2
, serine/threonine-protein kinase N2
, serine/threonine kinase 7
, p140 kinase
, protease-activated kinase 2
, protein kinase N2
, protein kinase C-related kinase 2
, serine/threonine-protein kinase N2-like