Carboxyl-terminal Phosphorylation Regulates the Function and Subcellular Localization of Protein Kinase C βII

Rice black-streaked dwarf virus (RBSDV) was known to be transmitted by the small brown planthopper (SBPH) in a persistent, circulative and propagative manner in nature. Here, we show that RBSDV major outer capsid protein (also known as P10) suppresses the protein kinase C (PKC) activity of SBPH through interacting with the receptor for activated protein kinase C 1 (LsRACK1). The N terminal of P10 (amino acids (aa) 1–270) and C terminal of LsRACK1 (aa 268–315) were mapped as crucial for the interaction. Confocal microscopy and subcellular fractionation showed that RBSDV P10 fused to enhanced green fluorescent protein formed vesicular structures associated with endoplasmic reticulum (ER) membranes in Spodoptera frugiperda nine cells. Our results also indicated that RBSDV P10 retargeted the initial subcellular localization of LsRACK1 from cytoplasm and cell membrane to ER and affected the function of LsRACKs to activate PKC. Inhibition of RACK1 by double stranded RNA-induced gene silencing significantly promoted the replication of RBSDV in SBPH. In addition, the PKC pathway participates in the antivirus innate immune response of SBPH. This study highlights that RACK1 negatively regulates the accumulation of RBSDV in SBPH through activating the PKC signalling pathway, and RBSDV P10 changes the subcellular localization of LsRACK1 and affects its function to activate PKC. This article is part of the theme issue ‘Biotic signalling sheds light on smart pest management’.

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The M-CSF receptor substrate and interacting protein FMIP is governed in its subcellular localization by protein kinase C-mediated phosphorylation, and thereby potentiates M-CSF-mediated differentiation

Oncogene ◽

10.1038/sj.onc.1207841 ◽

2004 ◽

Vol 23 (39) ◽

pp. 6581-6589 ◽

Cited By ~ 24

Author(s):

Annalisa Mancini ◽

Alexandra Koch ◽

Anthony D Whetton ◽

Teruko Tamura

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Subcellular Localization ◽

Interacting Protein ◽

Kinase C

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Yeast phenotype classifies mammalian protein kinase C cDNA mutants.

Molecular and Cellular Biology ◽

10.1128/mcb.13.8.4728 ◽

1993 ◽

Vol 13 (8) ◽

pp. 4728-4735 ◽

Cited By ~ 9

Author(s):

H Riedel ◽

L Su ◽

H Hansen

Keyword(s):

Protein Kinase C ◽

Catalytic Activity ◽

Protein Kinase ◽

Phorbol Ester ◽

Colony Size ◽

Receptor Protein ◽

Amino Terminal ◽

Kinase C ◽

Carboxyl Terminal ◽

Pkc Alpha

The phorbol ester receptor protein kinase C (PKC) gene family encodes essential mediators of eukaryotic cellular signals. Molecular dissection of their mechanisms of action has been limited in part by the lack of random mutagenesis approaches and by the complexity of signaling pathways in mammalian cells which involve multiple PKC isoforms. Here we present a rapid screen which permits the quantification of mammalian PKC activity phenotypically in the yeast Saccharomyces cerevisiae. Bovine PKC alpha cDNA is functionally expressed in S. cerevisiae. This results in a phorbol ester response: a fourfold increase in the cell doubling time and a substantial decrease in yeast colony size on agar plates. We have expressed pools of bovine PKC alpha cDNAs mutagenized by Bal 31 deletion of internal, amino-terminal, or carboxyl-terminal sequences and have identified three classes of mutants on the basis of their distinct yeast phenotypes. Representatives of each class were analyzed. An internal deletion of amino acids (aa) 172 to 225 displayed ligand-dependent but reduced catalytic activity, an amino-terminal truncation of aa 1 to 153 displayed elevated and ligand-independent activity, and a carboxyl-terminal 26-aa truncation (aa 647 to 672) lacked activity under any conditions. Additional mutations confirmed the distinct functional characteristics of these classes. Our data show that deletion of the V1 and C1 regions results in elevated basal catalytic activity which is still Ca2+ responsive. Internal deletions in the V2 and C2 regions do not abolish phorbol ester or Ca2+ regulation of PKC activity, suggesting that most of the C2 domain is not essential for phorbol ester stimulation and most of the regulatory domain is dispensable for Ca2+ regulation of PKC activity. These distinct activities od the PKC mutants correlate with a specific and proportional yeast phenotype and are quantified on agar plates by yeast colony size. This provides a phenotypic screen which is suitable to identity rare, randomly altered but active mammalian PKC mutants. It quantifies their catalytic and biological activities in response to PKC activators or inhibitors for a systematic mapping of PKC structure and function or PKC-drug interaction.

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Protein kinase C gamma interneurons in the rat medullary dorsal horn: Distribution and synaptic inputs to these neurons, and subcellular localization of the enzyme

The Journal of Comparative Neurology ◽

10.1002/cne.23407 ◽

2013 ◽

Vol 522 (2) ◽

pp. 393-413 ◽

Cited By ~ 15

Author(s):

Cédric Peirs ◽

Sudarshan Patil ◽

Rabia Bouali-Benazzouz ◽

Alain Artola ◽

Marc Landry ◽

...

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Subcellular Localization ◽

Dorsal Horn ◽

Synaptic Inputs ◽

Kinase C ◽

Medullary Dorsal Horn ◽

Protein Kinase C Gamma

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Subcellular localization of protein kinase C δ and ε affects transcriptional and post-transcriptional processes in four-cell mouse embryos

Reproduction ◽

10.1530/rep.1.00572 ◽

2005 ◽

Vol 130 (4) ◽

pp. 453-465 ◽

Cited By ~ 8

Author(s):

Hesam Dehghani ◽

Cara Reith ◽

Ann C Hahnel

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Subcellular Localization ◽

Cajal Bodies ◽

Message Processing ◽

Mrna Transcription ◽

Cell Stage ◽

Kinase C ◽

Sm Protein ◽

Small Nuclear Ribonucleoproteins

During mouse preimplantation development, two isozymes of protein kinase C (PKC), δ and ε, transiently localize to nuclei at the early four-cell stage. In order to study their functions at this stage, we altered the subcellular localization of these isozymes (ratio of nuclear to cytoplasmic concentrations) with peptides that specifically activate or inhibit translocation of each isozyme. The effects of altering nuclear concentration of each isozyme on transcription (5-bromouridine 5′-triphosphate (BrUTP) incorporation), amount and distribution of small nuclear ribonucleoproteins (snRNPs), nucleolar dynamics (immunocytochemistry for Smith antigen (Sm) protein) and the activity of embryonic alkaline phosphatase (EAP; histochemistry) were examined. We found that nuclear concentration of PKC ε correlated with total mRNA transcription. Higher nuclear concentrations of both PKC δ and ε decreased storage of snRNPs in Cajal bodies and decreased the number of nucleoli, but did not affect the nucleoplasmic concentration of snRNPs. Inhibiting translocation of PKC δ out of the nucleus at the early four-cell stage decreased cytoplasmic EAP activity, whereas inhibiting translocation of PKC ε increased EAP activity slightly. These results indicate that translocation of PKC δ and ε in and out of nuclei at the early four-cell stage in mice can affect transcription or message processing, and that sequestration of these PKC in nuclei can also affect the activity of a cytoplasmic protein (EAP).

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