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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Terms

 

Gene Review: 

PRKCE  -  protein kinase C, epsilon

Homo sapiens

Synonyms: PKCE, Protein kinase C epsilon type, nPKC-epsilon
 
 
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High impact information on PRKCE

  • In contrast, TEY phosphorylation induced by constitutively active MEK-1 was not effected by nPKC-epsilon, suggesting another position for this kinase within the cascade investigated [1].
  • Protein kinase C (PKC) assays and immunoblot analysis of calcium-dependent (cPKC) and calcium-independent (nPKC) isoforms revealed that nPKC-epsilon was strikingly absent in the mutant, which otherwise expressed in comparable amounts all other isotypes (cPKC-alpha, cPKC-beta, and nPKC-zeta) also present in the wild type [2].
  • In this condition, the translocation of cPKC alpha, nPKC delta and nPKC epsilon induced by TPA still occurred, however, that of cPKC alpha was reduced more than in the normal condition [3].
  • A particularly notable example is that promoter sequence analysis and real-time PCR assays support the predicted regulation of protein kinase C epsilon (Prkce) by cAMP responsive element binding protein 1 (Creb1) [4].
  • In addition to the clear difference between cPKC and nPKC, functional diversity among conventional PKCs has also been demonstrated; PKC gamma differs in its competence to mediate the signal toward transcriptional activation through TPA-responsive cis-acting elements from cPKC alpha and nPKC epsilon [5].
 

Biological context of PRKCE

 

Anatomical context of PRKCE

 

Associations of PRKCE with chemical compounds

  • Kinetic studies on seven subtypes of PKC further demonstrate a specific involvement of PKCE in this tyrosine phosphorylation/activation process [7].

References

  1. Protein kinase C isoforms involved in the transcriptional activation of cyclin D1 by transforming Ha-Ras. Kampfer, S., Windegger, M., Hochholdinger, F., Schwaiger, W., Pestell, R.G., Baier, G., Grunicke, H.H., Uberall, F. J. Biol. Chem. (2001) [Pubmed]
  2. Human leukemia K562 cell mutant (K562/OA200) selected for resistance to okadaic acid (protein phosphatase inhibitor) lacks protein kinase C-epsilon, exhibits multidrug resistance phenotype, and expresses drug pump P-glycoprotein. Zheng, B., Chambers, T.C., Raynor, R.L., Markham, P.N., Gebel, H.M., Vogler, W.R., Kuo, J.F. J. Biol. Chem. (1994) [Pubmed]
  3. Differential expression of protein kinase C isoforms in glial and neuronal cells. Translocation and down-regulation of PKC isoforms in C6 glioma and NG 108-15 hybrid cells: effects of extracellular Ca(2+)-depletion. Chen, C.C., Chang, J., Lin, W.W. Neurochem. Int. (1995) [Pubmed]
  4. Combining gene expression QTL mapping and phenotypic spectrum analysis to uncover gene regulatory relationships. Bao, L., Wei, L., Peirce, J.L., Homayouni, R., Li, H., Zhou, M., Chen, H., Lu, L., Williams, R.W., Pfeffer, L.M., Goldowitz, D., Cui, Y. Mamm. Genome (2006) [Pubmed]
  5. Structural and functional diversities of a family of signal transducing protein kinases, protein kinase C family; two distinct classes of PKC, conventional cPKC and novel nPKC. Ohno, S., Akita, Y., Hata, A., Osada, S., Kubo, K., Konno, Y., Akimoto, K., Mizuno, K., Saido, T., Kuroki, T. Adv. Enzyme Regul. (1991) [Pubmed]
  6. The myristoylated alanine-rich C-kinase substrate (MARCKS) is sequentially phosphorylated by conventional, novel and atypical isotypes of protein kinase C. Herget, T., Oehrlein, S.A., Pappin, D.J., Rozengurt, E., Parker, P.J. Eur. J. Biochem. (1995) [Pubmed]
  7. The naturally occurring PKC inhibitor sphingosine and tumor promoter phorbol ester potentially induce tyrosine phosphorylation/activation of oncogenic proline-directed protein kinase FA/GSK-3alpha in a common signalling pathway. Lee, S.C., Kuan, C.Y., Wen, Z.D., Yang, S.D. J. Protein Chem. (1998) [Pubmed]
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