PRKCE

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Protein kinase C, epsilon
Protein PRKCE PDB 1gmi.png
PDB rendering based on 1gmi.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols PRKCE ; PKCE; nPKC-epsilon
External IDs OMIM176975 MGI97599 HomoloGene48343 ChEMBL: 3582 GeneCards: PRKCE Gene
EC number 2.7.11.13
RNA expression pattern
PBB GE PRKCE 206248 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5581 18754
Ensembl ENSG00000171132 ENSMUSG00000045038
UniProt Q02156 P16054
RefSeq (mRNA) NM_005400 NM_011104
RefSeq (protein) NP_005391 NP_035234
Location (UCSC) Chr 2:
45.88 – 46.42 Mb
Chr 17:
86.17 – 86.66 Mb
PubMed search [1] [2]

Protein kinase C epsilon type is an enzyme that in humans is encoded by the PRKCE gene.[1][2]

Function[edit]

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This kinase has been shown to be involved in many different cellular functions, such as apoptosis, cardioprotection from ischemia, heat shock response, as well as insulin exocytosis.

Clinical significance[edit]

Knockout and molecular studies in mice suggest that this kinase is important for regulating behavioural response to morphine[3] and alcohol.[4][5] It also plays a role lipopolysaccharide (LPS)-mediated signaling in activated macrophages and in controlling anxiety-like behavior.[6]

Substrates and interactions[edit]

PKC-epsilon has a wide variety of substrates, including ion channels, other signalling molecules and cytoskeletal proteins.[7]

PKC-epsilon has been shown to interact with:

See also[edit]

References[edit]

  1. ^ Basta P, Strickland MB, Holmes W, Loomis CR, Ballas LM, Burns DJ (Nov 1992). "Sequence and expression of human protein kinase C-epsilon". Biochim Biophys Acta 1132 (2): 154–60. doi:10.1016/0167-4781(92)90006-l. PMID 1382605. 
  2. ^ Lehel C, Olah Z, Jakab G, Anderson WB (Apr 1995). "Protein kinase C epsilon is localized to the Golgi via its zinc-finger domain and modulates Golgi function". Proc Natl Acad Sci U S A 92 (5): 1406–10. doi:10.1073/pnas.92.5.1406. PMC 42528. PMID 7877991. 
  3. ^ Newton PM, Kim JA, McGeehan AJ, Paredes JP, Chu K, Wallace MJ, Roberts AJ, Hodge CW, Messing RO (June 2007). "Increased response to morphine in mice lacking protein kinase C epsilon". Genes Brain Behav. 6 (4): 329–38. doi:10.1111/j.1601-183X.2006.00261.x. PMID 16899053. 
  4. ^ Newton PM, Messing RO (January 2006). "Intracellular signaling pathways that regulate behavioral responses to ethanol". Pharmacol. Ther. 109 (1-2): 227–37. doi:10.1016/j.pharmthera.2005.07.004. PMID 16102840. 
  5. ^ Amygdala protein kinase C epsilon controls alcohol consumption http://www3.interscience.wiley.com/journal/122210376/abstract
  6. ^ "Entrez Gene: PRKCE protein kinase C, epsilon". 
  7. ^ Newton PM, Messing RO (April 2010). "The substrates and binding partners of protein kinase Cepsilon". Biochem. J. 427 (2): 189–96. doi:10.1042/BJ20091302. PMC 2966297. PMID 20350291. 
  8. ^ a b c d England K, Ashford D, Kidd D, Rumsby M (June 2002). "PKC epsilon is associated with myosin IIA and actin in fibroblasts". Cell. Signal. 14 (6): 529–36. doi:10.1016/S0898-6568(01)00277-7. PMID 11897493. 
  9. ^ a b Liedtke CM, Yun CH, Kyle N, Wang D (June 2002). "Protein kinase C epsilon-dependent regulation of cystic fibrosis transmembrane regulator involves binding to a receptor for activated C kinase (RACK1) and RACK1 binding to Na+/H+ exchange regulatory factor". J. Biol. Chem. 277 (25): 22925–33. doi:10.1074/jbc.M201917200. PMID 11956211. 
  10. ^ Baines CP, Song CX, Zheng YT, Wang GW, Zhang J, Wang OL, Guo Y, Bolli R, Cardwell EM, Ping P (May 2003). "Protein kinase Cepsilon interacts with and inhibits the permeability transition pore in cardiac mitochondria". Circ. Res. 92 (8): 873–80. doi:10.1161/01.RES.0000069215.36389.8D. PMID 12663490. 
  11. ^ Gannon-Murakami L, Murakami K (June 2002). "Selective association of protein kinase C with 14-3-3 zeta in neuronally differentiated PC12 Cells. Stimulatory and inhibitory effect of 14-3-3 zeta in vivo". J. Biol. Chem. 277 (26): 23116–22. doi:10.1074/jbc.M201478200. PMID 11950841. 

Further reading[edit]