The carboxyl terminus of protein kinase c provides a switch to regulate its interaction with the phosphoinositide-dependent kinase, PDK-1.
about
The phosphatase PHLPP controls the cellular levels of protein kinase CDynamics and Membrane Interactions of Protein Kinase CThe Novel PKCθ from Benchtop to ClinicHigh resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site.The C-terminal V5 domain of Protein Kinase Cα is intrinsically disordered, with propensity to associate with a membrane mimeticPeripheral inflammation induces tumor necrosis factor dependent AMPA receptor trafficking and Akt phosphorylation in spinal cord in addition to pain behaviorAcute ethanol administration rapidly increases phosphorylation of conventional protein kinase C in specific mammalian brain regions in vivoStructural basis of protein kinase C isoform functionThe turn motif is a phosphorylation switch that regulates the binding of Hsp70 to protein kinase C.The adaptor protein Grb14 regulates the localization of 3-phosphoinositide-dependent kinase-1.Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigmSignalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions.Complex regulation of PKCβ2 and PDK-1/AKT by ROCK2 in diabetic heart.The hallmark of AGC kinase functional divergence is its C-terminal tail, a cis-acting regulatory module.Peptidyl-prolyl isomerase Pin1 controls down-regulation of conventional protein kinase C isozymesTranslocation of PKC[theta] in T cells is mediated by a nonconventional, PI3-K- and Vav-dependent pathway, but does not absolutely require phospholipase CPhosphoinositide-dependent kinase-1 and protein kinase Cδ contribute to endothelin-1 constriction and elevated blood pressure in intermittent hypoxia1-42 β-amyloid peptide requires PDK1/nPKC/Rac 1 pathway to induce neuronal death.Protein kinase C activation and its role in kidney disease.Regulation of PI3K by PKC and MARCKS: Single-Molecule Analysis of a Reconstituted Signaling PathwayInsight into intra- and inter-molecular interactions of PKC: design of specific modulators of kinase function.Protein kinase Czeta represses the interleukin-6 promoter and impairs tumorigenesis in vivo.Regulation of a third conserved phosphorylation site in SGK1The chaperones Hsp90 and Cdc37 mediate the maturation and stabilization of protein kinase C through a conserved PXXP motif in the C-terminal tail.The life and death of protein kinase C.Protein kinase C, focal adhesions and the regulation of cell migration.Erk1/2-dependent phosphorylation of PKCalpha at threonine 638 in hippocampal 5-HT(1A) receptor-mediated signaling.Interaction with AKAP79 modifies the cellular pharmacology of PKC.A chimeric mechanism for polyvalent trans-phosphorylation of PKA by PDK1.Parvovirus interference with intracellular signalling: mechanism of PKCeta activation in MVM-infected A9 fibroblasts.Identification of acidic amino acid residues in the protein kinase C alpha V5 domain that contribute to its insensitivity to diacylglycerol.Phosphoinositide-dependent protein kinase-1 (PDK1)-independent activation of the protein kinase C substrate, protein kinase D.Invariant Leu preceding turn motif phosphorylation site controls the interaction of protein kinase C with Hsp70.The in vivo role of PtdIns(3,4,5)P3 binding to PDK1 PH domain defined by knockin mutation.The tumor promoter-activated protein kinase Cs are a system for regulating filopodia.Regulation of protein kinase C-related protein kinase 2 (PRK2) by an intermolecular PRK2-PRK2 interaction mediated by Its N-terminal domain.Protein kinase d inhibitors uncouple phosphorylation from activity by promoting agonist-dependent activation loop phosphorylation.Hydrophobic motif phosphorylation coordinates activity and polar localization of the Neurospora crassa nuclear Dbf2-related kinase COT1.Fused protein of deltaPKC activation loop and PDK1-interacting fragment (deltaAL-PIF) functions as a pseudosubstrate and an inhibitory molecule for PDK1 when expressed in cells.Predominant contribution of DGKζ over DGKα in the control of PKC/PDK-1-regulated functions in T cells.
P2860
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P2860
The carboxyl terminus of protein kinase c provides a switch to regulate its interaction with the phosphoinositide-dependent kinase, PDK-1.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh
2001年學術文章
@zh-hant
name
The carboxyl terminus of prote ...... itide-dependent kinase, PDK-1.
@en
type
label
The carboxyl terminus of prote ...... itide-dependent kinase, PDK-1.
@en
prefLabel
The carboxyl terminus of prote ...... itide-dependent kinase, PDK-1.
@en
P2093
P2860
P356
P1476
The carboxyl terminus of prote ...... itide-dependent kinase, PDK-1.
@en
P2093
P2860
P304
19588-19596
P356
10.1074/JBC.M101357200
P407
P577
2001-03-16T00:00:00Z