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PRKCE

This article was updated by an external expert under a dual publication model. The corresponding peer-reviewed article was published in the journal Gene. Click to view.
From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
This article is about the enzyme. For the OAuth security extension PKCE, seeOAuth § Security_issues.
PRKCE
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

2WH0

Identifiers
AliasesPRKCE, PKCE, nPKC-epsilon, protein kinase C epsilon
External IDsOMIM:176975;MGI:97599;HomoloGene:48343;GeneCards:PRKCE;OMA:PRKCE - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for PRKCE
Genomic location for PRKCE
Band2p21Start45,651,345bp[1]
End46,187,990bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for PRKCE
Genomic location for PRKCE
Band17|17 E4Start86,475,213bp[2]
End86,965,347bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • buccal mucosa cell

  • sural nerve

  • lateral nuclear group of thalamus

  • Parietal Lobe

  • postcentral gyrus

  • right lung

  • middle temporal gyrus

  • sperm

  • superior frontal gyrus

  • entorhinal cortex
Top expressed in
  • anterior amygdaloid area

  • subiculum

  • lateral septal nucleus

  • olfactory tubercle

  • dentate gyrus

  • prefrontal cortex

  • hippocampus proper

  • dentate gyrus of hippocampal formation granule cell

  • ventromedial nucleus

  • medial dorsal nucleus
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
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: 45.65 – 46.19 MbChr 17: 86.48 – 86.97 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein kinase C epsilon type (PKCε) is anenzyme that in humans is encoded by thePRKCEgene.[5][6] PKCε is anisoform of the largePKC family ofprotein kinases that play many roles in different tissues. Incardiac muscle cells, PKCε regulatesmuscle contraction through its actions atsarcomeric proteins, and PKCε modulates cardiac cellmetabolism through its actions atmitochondria. PKCε is clinically significant in that it is a central player incardioprotection againstischemic injury and in the development ofcardiac hypertrophy.

Structure

[edit]

HumanPRKCE gene (Ensembl ID: ENSG00000171132) encodes theprotein PKCε (Uniprot ID: Q02156), which is 737 amino acids in length with a molecular weight of 83.7 kDa. The PKC family ofserine-threoninekinases contains thirteen PKCisoforms, and eachisoform can be distinguished by differences inprimary structure,gene expression, subcellular localization, and modes of activation.[7] The epsilonisoform of PKC is abundantly expressed in adultcardiomyocytes,[8][9][10][11] being the most highly expressed of all novel isoforms, PKC-δ, -ζ, and –η.[12] PKCε and other PKCisoforms requirephosphorylation at sitesThreonine-566,Threonine-710, andSerine-729 forkinase maturation.[13] The epsilonisoform ofPKC differs from otherisoforms by the position of the C2,pseudosubstrate, and C1 domains; varioussecond messengers in different combinations can act on the C1 domain to direct subcellular translocation of PKCε.[9][14]

Receptors for activated C-kinase (RACK) have been found to anchor activePKC in close proximity tosubstrates.[15] PKCε appears to have preferred affinity to the (RACK/RACK2) isoform; specifically, the C2 domain of PKCε atamino acids 14–21 (also known as εV1-2) binds (RACK/RACK2), and peptide inhibitors targeting εV1-2 inhibit PKCε translocation and function incardiomyocytes,[16] while peptide agonists augment translocation.[17] It has been demonstrated that altering the dynamics of the (RACK/RACK2) and (RACK1) interaction with PKCε can influencecardiac muscle phenotypes.[18]

Activated PKCε translocates to various intracellular targets.[13][19] Incardiac muscle, PKCε translocates tosarcomeres atZ-lines followingα-adrenergic andendothelin (ET)A-receptor stimulation.[9][20] A myriad ofagonists have also been shown to induce the translocation of PKCε from thecytosolic to particulate fraction incardiomyocytes, including but not limited toPMA ornorepinephrine;[9]arachidonic acid;[21]ET-1 andphenylephrine;[22][23]angiotensin II anddiastolic stretch;[24]adenosine;[25]hypoxia and Akt-induced stem cell factor;[26]ROS generated via pharmacologic activation of themitochondrial potassium-sensitive ATP channel (mitoK(ATP))[27] and the endogenousG-protein coupled receptorligand,apelin.[28]

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 messengerdiacylglycerol. PKC family membersphosphorylate 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 forphorbol 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 asapoptosis, cardioprotection fromischemia,heat shock response, as well as insulinexocytosis.

Cardiac muscle sarcomeric contractile function

[edit]

PKCε translocates tocardiac musclesarcomeres and modulatescontractility of themyocardium. PKCε bindsRACK2 atZ-lines with an EC50 of 86 nM;[29] PKCε also binds atcostameres tosyndecan-4.[30] PKCε has been shown to bindF-actin inneurons, which modulates synaptic function and differentiation;[31][32] however it is unknown whether PKCε bindssarcomericactin in muscle cells.Sarcomeric proteins have been identified in PKCε signaling complexes, includingactin,cTnT,tropomyosin,desmin, andmyosin light chain-2; in mice expressing a constitutively-active PKCε, allsarcomeric proteins showed greater association with PKCε, and thecTnT,tropomyosin,desmin andmyosin light chain-2 exhibited changes in post-translational modifications.[33]

PKCε binds andphosphorylatescardiac troponin I (cTnI) andcardiac troponin T (cTnT) in complex withtroponin C (cTnC);[34]phosphorylation on cTnI at residuesSerine-43,Serine-45, andThreonine-144 cause depression of actomyosin S1 MgATPase function.[35][36] These studies were further supported by those performed in isolated, skinnedcardiac muscle fibers, showing that in vitrophosphorylation ofcTnI by PKCε orSerine-43/45 mutation toGlutamate to mimicphosphorylation desensitized myofilaments tocalcium and decreased maximal tension and filament sliding speed.[37] Phosphorylation oncTnI atSerine-5/6 also showed this depressive effect.[38] Further support was gained from in vivo studies in which mice expressing a mutant cTnI (Serine43/45Alanine) exhibited enhanced cardiaccontractility.[39]

Cardiac muscle mitochondrial metabolism and function

[edit]

In addition tosarcomeres, PKCε also targetscardiacmitochondria.[33][40]Proteomic analysis of PKCε signaling complexes in mice expressing a constitutively-active, overexpressed PKCε identified several interacting partners atmitochondria whose protein abundance andposttranslational modifications were altered in thetransgenic mice.[33] This study was the first to demonstrate PKCε at theinner mitochondrial membrane,[33] and it was found that PKCε binds severalmitochondrial proteins involved inglycolysis,TCA cycle,beta oxidation, andion transport.[41] However, it remained unclear how PKCε translocates from theouter toinner mitochondrial membrane until Budas et al. discovered thatheat shock protein 90 (Hsp90) coordinates with thetranslocase of the outer mitochondrial membrane-20 (Tom20) to translocate PKCε following a preconditioning stimulus.[42][43] Specifically, a sevenamino acid peptide, termed TAT-εHSP90, homologous to theHsp90 sequence within the PKCε C2 domain induced translocation of PKCε to theinner mitochondrial membrane andcardioprotection.[42]

PKCε has also been shown to play a role in modulatingmitochondrial permeability transition (MPT); the addition of PKCε tocardiomyocytes inhibits MPT,[40] though the mechanism is unclear. Initially, PKCε was thought to protect mitochondria from MPT through its association withVDAC1,ANT, andhexokinase II;[40] however, genetic studies have since ruled this out[44][45] and subsequent studies have identified the F0/F1ATP synthase as a core inner mitochondrial membrane component[46][47][48][49] and Bax and Bak as potential outer membrane components[50] These findings have opened up new avenues of investigation for the role of PKCε atmitochondria. Several likely targets of PKCε action affecting MPT have been discovered. PKCε interacts withERK,JNKs andp38, and PKCε directly or indirectlyphosphorylatesERK and subsequentlyBad.[51] PKCε also interacts withBax incancer cells, and PKCε modulates its dimerization and function.[52][53] Activation of PKCε with the specific activator, εRACK, prior to ischemic injury has shown to be associated withphosphorylation of the F0/F1ATP synthase.[54] Moreover, the modulatory component,ANT is regulated by PKCε.[40] These data suggest that PKCε may act at multiple modulatory targets of MPT function; further studies are required to unveil the specific mechanism.

Clinical significance

[edit]

Cardiac hypertrophy and heart failure

[edit]

Findings of PKCεphosphorylation in animal models have been verified in humans; PKCεphosphorylatescTnI,cTnT, andMyBPC and depresses the sensitivity of myofilaments to calcium.[55] PKCε induction occurs in the development ofcardiac hypertrophy, following stimuli such asmyotrophin,[56] mechanical stretch andhypertension.[57] The precise role of PKCε inhypertrophic induction has been debated. The inhibition of PKCε during transition fromhypertrophy toheart failure enhances longevity;[58] however, inhibition of PKCε translocation via a peptide inhibitor increases cardiomyocyte size and expression ofhypertrophic gene panel.[59] A role forfocal adhesion kinase atcostameres in strain-sensing and modulation of sarcomere length has been linked to hypertrophy. The activation ofFAK by PKCε occurs following ahypertrophic stimulus, which modulatessarcomere assembly.[60][61] PKCε also regulatesCapZ dynamics following cyclic strain.[62]

Transgenic studies involving PKCε have also shed light on its function in vivo. Cardiac-specific overexpression of constitutively-active PKCε (9-fold increase in PKCε protein, 4-fold increase in activity) inducedcardiac hypertrophy characterizes by enhanced anterior and posteriorleft ventricular wall thickness.[63] A later study unveiled that the aging of PKCεtransgenic mice brought ondilated cardiomyopathy andheart failure by 12 months of age,[64]] characterized by a preservedFrank-Starling mechanism and exhausted contractile reserve.[65] Crossing PKCεtransgenic mice with mutantcTnI mice lacking PKCεphosphorylation sites (Serine-43/Serine-45 mutated toAlanine) attenuated the contractile dysfunction and hypertrophic marker expression, offering critical mechanistic insights.[66]

Cardioprotection against Ischemic injury

[edit]

JM Downey was the first to introduce the role ofPKC incardioprotection againstischemia-reperfusion injury in 1994,;[67] this seminal idea stimulated a series of studies which examined the differentisoforms ofPKC. PKCε has been demonstrated to be a central player inpreconditioning in multiple independent studies, with its best known actions atcardiacmitochondria. It was first demonstrated by Ping et al. that in five distinctpreconditioning regimens in conscious rabbits, the epsilon isoform ofPKC specifically translocated from thecytosolic to particulate fraction.[12][68] This finding was validated by multiple independent studies occurring shortly thereafter,[69][70] and has since been observed in multiple animal models[71][72][73] and human tissue,[74] as well as in studies employing transgenesis and PKCε activators/inhibitors.[75]

Mitochondrial targets of PKCε involved incardioprotection have been actively pursued, since the translocation of PKCε to mitochondria following protective stimuli is one of the most well-accepted cardioprotective paradigms. PKCε has been shown to target andphosphorylatealcohol dehydrogenase 2 (ALDH2) following preconditioning stimuli, which increased the activity ofALDH2 and reducedinfarct size.[76][77] Moreover, PKCε interacts withcytochrome c oxidase subunit IV (COIV), and preconditioning stimuli evokedphosphorylation of COIV and stabilization of COIV protein and activity.[78] ThemitochondrialATP-sensitive potassium channel (mitoK(ATP)) also interacts with PKCε;phosphorylation ofmitoK(ATP) following preconditioning stimuli potentiates channel opening.[79][80] PKCε modulates the interaction between subunitKir6.1 ofmitoK(ATP) andconnexin-43, whose interaction conferscardioprotection.[81] Lastly, several mitochondrialmetabolic targets of PKCεphosphorylation involved incardioprotection following activation with εRACK have been identified, includingmitochondrial respiratory complexes I, II and III, as well as proteins involved inglycolysis,lipid oxidation,ketone body metabolism andheat shock proteins.[54]

The role of PKCε acting in non-mitochondrial regions ofcardiomyocytes is less well understood, though some studies have identifiedsarcomeric targets. PKCε translocation tosarcomeres andphosphorylation ofcTnI andcMyBPC is involved in theκ-opioid- andα-adrenergic-dependent preconditioning that slowsmyosin cycling rate, thus protecting the contractile apparatus from damage.[82][83] Activation of PKCε by εRACK prior toischemia was also found tophosphorylateVentricular myosin light chain-2,[54] however the functional significance remains elusive.Actin-capping protein, CapZ appears to affect the localization of PKCε toZ-lines[84] and modulates thecardiomyocyte response toischemic injury.Cardioprotection in mice with reduction ofCapZ showed enhancement in PKCε translocation tosarcomeres,[85] thus suggesting thatCapZ may compete with PKCε for the binding of RACK2.

Other functions

[edit]

Knockout and molecular studies in mice suggest that this kinase is important for regulating behavioural response to morphine[86] and alcohol.[87][88] It also plays a role lipopolysaccharide (LPS)-mediated signaling in activated macrophages and in controlling anxiety-like behavior.[89]

Substrates and interactions

[edit]

PKC-epsilon has a wide variety of substrates, includingion channels, other signalling molecules andcytoskeletal proteins.[90]

PKC-epsilon has been shown tointeract with:

See also

[edit]

Notes

[edit]

Journal
The 2016 version of this article was updated by an external expert under a dual publication model. The correspondingacademic peer reviewed article was published inGene and can be cited as:
Sarah B Scruggs; Ding Wang; Peipei Ping (13 June 2016)."PRKCE gene encoding protein kinase C-epsilon-Dual roles at sarcomeres and mitochondria in cardiomyocytes".Gene. Gene Wiki Review Series.590 (1):90–96.doi:10.1016/J.GENE.2016.06.016.ISSN 0378-1119.PMC 5366072.PMID 27312950.Wikidata Q38867832.

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Further reading

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External links

[edit]
  • Overview of all the structural information available in thePDB forUniProt:Q02156 (Protein kinase C epsilon type) at thePDBe-KB.
PDB gallery
  • 1gmi: STRUCTURE OF THE C2 DOMAIN FROM NOVEL PROTEIN KINASE C EPSILON
    1gmi: STRUCTURE OF THE C2 DOMAIN FROM NOVEL PROTEIN KINASE C EPSILON
Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
  • -
IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)
  • -
Tropomyosin kinase (EC 2.7.11.28)
  • -
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)
  • -
Receptor protein serine/threonine kinase (EC 2.7.11.30)
MAP2K
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