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PRKCI (protein kinase C, iota)

Identity

Other namesDXS1179E
nPKC-iota
PKCI
HGNC (Hugo) PRKCI
LocusID (NCBI) 5584
Location 3q26.2
Location_base_pair Starts at 169940220 and ends at 170023770 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order The PRKCI gene is located between the polyhomeotic homolog 3 gene in centromeric position and the SKI-like oncogene in telomeric position (according to GeneLoc).
 
  Location sequence of PRKCI on Chromosome 3. PRKCI gene is indicated by red arrow.

DNA/RNA

 
  Exon-intron structure of the PRKCI gene. Blue vertical bars correspond to exons, green bar represents 5'UTR and orange 3'UTR.
Description The PRKCI gene is composed of 18 exons and spans 83618 bases on the plus strand.
Transcription The PRKCI transcript (NM_002740) contains 4884 bases and the open reading frame spans from 239 to 2029.
Pseudogene There is a single exon pseudogene mapped on chromosome X.

Protein

 
  Schematic diagram showing the domain structure of PKCι. PB-1 Phox-Bem1; PS: auto-inhibitory pseudosubstrate sequence.
Description PKCι consist of 596 amino acids and has a molecular mass of 68262 Da. PKCι is a member of the PKCs, a diverse family of lipid dependent serine/threonine kinases. PKCι activity can be regulated by lipid second messengers (ceramide, phosphatidylinositol 3,4,5-P3, and phosphatidic acid), phosphoinositide-dependent kinase (PDK1), tyrosine phosphorylation and specific protein-protein interactions. The PB1 domain within the N-terminal regulatory domain mediates protein-protein interactions between PKCι and other PB1 domain containing proteins such as ZIP/p62 (Hirano et al., 2004; Puls et al., 1997), Par-6 (partitioning-defective 6) (Joberty et al., 2000; Lin et al., 2000; Noda et al., 2001; Qiu et al., 2000) and MEK5 (MAPK (mitogen-activated protein kinase)/ERK (extracellular-signal-regulated kinase) kinase 5) (Diaz-Meco and Moscat, 2001; Hirano et al., 2004). In the inactive state, the PKCι PS is positioned in the substrate binding cavity in the kinase domain and is displaced upon PKCι activation. Phosphatidylserine binds the C1 domain to anchor PKCι to the membrane. The PKCι catalytic domain is subdivided into the C3 and C4 domains that mediate ATP-binding and substrate binding.
Expression PKCι is widely expressed with varying levels in different tissues (Selbie et al., 1993).
Localisation PKCι is mainly expressed in the cytoplasm. PKCι is translocated to the cell membrane in response to second messengers and colocalizes with p62/ZIP in lysosome-targeted endosomes (Sanchez et al., 1998). Src phosphorylation leads to translocation of PKCι into the nucleus (White et al., 2002) where it forms a complex with Cdk7 (Win and Acevedo-Duncan, 2008).
Function PKCι is a lipid-dependent, serine/threonine kinase. PKCι participates a number of signaling pathways that regulate cell survival (Sanz et al., 1999; Wooten et al., 1999; Xie et al., 2000), differentiation (Wooten et al., 2000), polarity (Joberty et al., 2000), and microtubule dynamics in the early secretory pathway (Tisdale, 2002).
Homology PRKCI is highly evolutionarily conserved. PKCι and PKCζ exhibit 72% overall amino acid sequence homology and 86% identity within the kinase domain. PKCι shows less homology with the other PKC isoform, with less than 53% identity in the highly conserved catalytic domain (Selbie et al., 1993).

Mutations

Germinal No germline mutations in the PRKCI gene have been reported.
Somatic The PKCι gene is amplified as part of the 3q26 amplicon in lung (Regala et al., 2005b), esophageal (Yang et al., 2008) and ovarian (Eder et al., 2005; Zhang et al., 2006) cancers. A P118L mutation was found in a metastatic melanoma sample (Greenman et al., 2007).

Implicated in

Entity Various cancers
Note PKCι overexpression has been observed in numerous human cancers including cancers of the lung (Regala et al., 2005b), pancreas (Scotti et al., 2010), stomach (Takagawa et al., 2010), colon (Murray et al., 2004), esophagus (Yang et al., 2008), liver (Du et al., 2009), bile duct (Li et al., 2008), breast (Kojima et al., 2008), ovary (Weichert et al., 2003; Eder et al., 2005; Zhang et al., 2006), prostate (Ishiguro et al., 2009), and brain (Patel et al., 2008). PKCι is itself an oncogene, which appears to be activated through tumor-specific overexpression. In addition, however, PKCι is activated downstream of other oncogenes including oncogenic Ras, Bcr-Abl and Src.
  
Entity Non Small Cell Lung Cancer (NSCLC)
Prognosis Elevated levels of PKCι expression correlate with poor clinical outcome in NSCLC patients (Regala et al., 2005b).
Cytogenetics The PRKCI gene is amplified as part of the 3q26 amplicon in NSCLC.
Oncogenesis PKCι is an oncogene in NSCLC. PRKCI is amplified as part of the 3q26 amplicon in NSCLC and amplication drives PKCι overexpression in NSCLC cell lines and primary NSCLC tumours. PKCι is required for transformed (anchorage-independent) growth and invasion of human NSCLC cells (Frederick et al., 2008; Regala et al., 2005a). Disruption of the Prkci gene inhibits oncogenic Kras induced expansion and transformation of tumor-initiating, lung stem-like cells. Consequently, genetic loss of Prkci dramatically inhibits Kras-initiated hyperplasia and subsequent lung tumor formation in vivo. PKCι enhances resistance of NSCLC to NNK-induced apoptosis by phosphorylating the pro-apoptotic protein BAD (Jin et al., 2005). PKCι forms an oncogeneic complex with Par6 that activates a Rac1-Mek-Erk signaling axis that drives the transformed growth and invasion of NSCLC cells in vitro (Frederick et al., 2008; Regala et al., 2005a) and tumorigenicity in vivo (Regala et al., 2005a). PKCι and the oncogene ECT2 are genetically linked through coordinate gene amplification as part of the 3q26 amplicon in NSCLC tumors (Justilien and Fields, 2009). PKCι phosphorylates Ect2 and forms an oncogenic PKCι-Par6-Ect2 complex that drives NSCLC cell transformation by activating Rac1 (Justilien and Fields, 2009; Justilien et al., 2011). Expression of MMP10 is regulated through the PKCι-Par6-Rac1 signaling axis and MMP10 represents a key downstream effector in PKCι mediated transformation in lung cancer cells that is required for transformed growth and invasion (Frederick et al., 2008). PKCι also regulates expression of COPB2, ELF3, RFC4, and PLS1 in primary lung adenocarcinoma (Erdogan et al., 2009). The PKCι inhibitor aurothiomalate (ATM) disrupts the PB1-PB1 domain interaction between PKCι and Par6 and inhibits PKCι-mediated Rac1 activation and blocks anchorage-independent growth of NSCLC cells in vitro and tumorigenicity in vivo (Erdogan et al., 2006; Stallings-Mann, 2006).
  
Entity Colon cancer
Oncogenesis PKCι expression is elevated in human colon tumors, AOM-induced colon tumors in mice (Murray et al., 2004) and intestinal tumors in APCMin/+ mice (Murray et al., 2009; Oster and Leitges, 2006). Expression of caPKCι in the colonic epithelium of mice led to an increase in the number of AOM-induced colon tumors, and promoted tumor progression from benign adenoma to malignant intramucosal carcinoma (Murray et al., 2004) PKCι is required for oncogenic Ras-mediated transformation of the intestinal epithelium in vitro and in vivo. PKCι is also required for the formation of intestinal tumors in APCMin/+ mice (Murray et al., 2009).
  
Entity Pancreatic cancer
Prognosis PKCι overexpression predicts poor survival in pancreatic cancer patients (Scotti et al., 2010).
Oncogenesis PKCι is significantly overexpressed in human pancreatic cancer. Knock down of PKCι expression using lentiviral-mediated shRNA blocked transformed (anchorage-independent) growth and invasion of human Pancreatic Ductal Adenocarcinoma (PDAC) cells (Scotti et al., 2010). Disruption of PKCι expression also blocks tumorigenicity of PDAC cell tumors injected orthotopically into the pancreas (Scotti et al., 2010). Analysis of human PDAC cells after orthotopic injection into the mouse pancreas revealed that PKCι-deficient tumor cells yielded significantly smaller tumors and significantly fewer metastases to the kidney, liver, diaphragm and mesentery (Scotti et al., 2010). The Rac1-MEK/ERK1/2 signaling axis is required for PKCiota-mediated transformed growth and cellular invasion of PDAC cells (Scotti et al., 2010).
  
Entity Ovarian cancer
Prognosis PKCι expression is a strong predictor of survival when combined in a multi-variate analysis with tumor cyclin E expression (Eder et al., 2005).
Cytogenetics The PRKCI gene is amplified as part of the 3q26 amplicon in ovarian cancer (Eder et al., 2005).
Oncogenesis PKCι is frequently overexpressed in patients with ovarian cancer (Eder et al., 2005; Weichert et al., 2003; Zhang et al., 2006). PKCι expression in ovarian cancer patients correlates with tumor stage suggesting the involvement of PKCι in tumor progression and aggressiveness (Eder et al., 2005; Weichert et al., 2003; Zhang et al., 2006). Decreased PKCι expression reduced anchorage-independent growth of ovarian cancer cells, whereas overexpression of PKCι promoted murine ovarian surface epithelium transformation (Zhang et al., 2006).
  
Entity Chronic myelogenous leukemia
Oncogenesis PKCι is highly expressed in human K562 leukemia cells and functions as a survival gene in chronic myelogenous leukemia (CML). The chimeric tyrosine kinase oncogene Bcr-Abl activates a Ras/Mek/Erk signaling pathway that stimulates PKCι expression through an Elk1 transcription factor site in the proximal promoter of PKCι (Gustafson et al., 2004). Bcr-Abl activation of PKCι is necessary and sufficient to mediate apoptotic resistance to chemotherapy in K562 CML cells (Murray and Fields, 1997).
  
Entity Gliomas
Oncogenesis PKCι is overexpressed in glioblastoma multiforme. PKCι is required for survival and chemoresistance of glioblastoma cells. Genetic disruption of PKCι expression results in sensitization of glioblastoma cells to cisplatin (Baldwin et al., 2008). RNAi mediated depletion of PKCι also blocks the proliferative and invasive properties of glioma cell lines in vitro (Baldwin et al., 2008; Patel et al., 2008). PKCι promotes survival in glioblastoma cells through attenuation of p38 mitogen-activated protein kinase signaling that protects these cells against cytotoxicity to chemotherapeutic agents (Baldwin et al., 2008).
  
Entity Esophageal cancer
Cytogenetics PRKCI gene is amplified as part of the 3q26 amplicon (Yang et al., 2008).
Oncogenesis PRKCI is amplified in 53% of esophageal squamous cell carcinomas (ESCC) and PKCι protein expression correlated with PRKCI gene amplification in these tumors (Yang et al., 2008). Examination of clinicopathologic features of ESCC tumors revealed a significant correlation between PRKCI expression and larger tumor size, later stage and lymph node metastasis suggesting that PRKCI overexpression is a hallmark of tumor progression and metastasis in ESCC (Yang et al., 2008).
  

External links

Nomenclature
HGNC (Hugo)PRKCI   9404
Cards
AtlasPRKCIID41857ch3q26
Entrez_Gene (NCBI)PRKCI  5584  protein kinase C, iota
GeneCards (Weizmann)PRKCI
Ensembl (Hinxton)ENSG00000163558 [Gene_View]  chr3:169940220-170023770 [Contig_View]  PRKCI [Vega]
ICGC DataPortalENSG00000163558
cBioPortalPRKCI
AceView (NCBI)PRKCI
Genatlas (Paris)PRKCI
WikiGenes5584
SOURCE (Princeton)NM_002740
Genomic and cartography
GoldenPath (UCSC)PRKCI  -  3q26.2   chr3:169940220-170023770 +  3q26.3   [Description]    (hg19-Feb_2009)
EnsemblPRKCI - 3q26.3 [CytoView]
Mapping of homologs : NCBIPRKCI [Mapview]
OMIM600539   
Gene and transcription
Genbank (Entrez)AB451443 AI521422 AK315342 BC022016 BC042405
RefSeq transcript (Entrez)NM_002740
RefSeq genomic (Entrez)AC_000135 NC_000003 NC_018914 NT_005612 NW_001838884 NW_004929311
Consensus coding sequences : CCDS (NCBI)PRKCI
Cluster EST : UnigeneHs.478199 [ NCBI ]
CGAP (NCI)Hs.478199
Alternative Splicing : Fast-db (Paris)GSHG0021312
Alternative Splicing GalleryENSG00000163558
Gene ExpressionPRKCI [ NCBI-GEO ]     PRKCI [ SEEK ]   PRKCI [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP41743 (Uniprot)
NextProtP41743  [Medical]
With graphics : InterProP41743
Splice isoforms : SwissVarP41743 (Swissvar)
Catalytic activity : Enzyme2.7.11.13 [ Enzyme-Expasy ]   2.7.11.132.7.11.13 [ IntEnz-EBI ]   2.7.11.13 [ BRENDA ]   2.7.11.13 [ KEGG ]   
Domaine pattern : Prosite (Expaxy)AGC_KINASE_CTER (PS51285)    PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_ST (PS00108)    ZF_DAG_PE_1 (PS00479)    ZF_DAG_PE_2 (PS50081)   
Domains : Interpro (EBI)AGC-kinase_C [organisation]   DAG/PE-bd [organisation]   Kinase-like_dom [organisation]   OPR_PB1 [organisation]   PKC_zeta [organisation]   Pkinase_C [organisation]   Prot_Kinase_C-like_PE/DAG-bd [organisation]   Prot_kinase_dom [organisation]   Protein_kinase_ATP_BS [organisation]   Ser/Thr_dual-sp_kinase_dom [organisation]   Ser/Thr_kinase_AS [organisation]  
Related proteins : CluSTrP41743
Domain families : Pfam (Sanger)C1_1 (PF00130)    PB1 (PF00564)    Pkinase (PF00069)    Pkinase_C (PF00433)   
Domain families : Pfam (NCBI)pfam00130    pfam00564    pfam00069    pfam00433   
Domain families : Smart (EMBL)C1 (SM00109)  PB1 (SM00666)  S_TK_X (SM00133)  S_TKc (SM00220)  
DMDM Disease mutations5584
Blocks (Seattle)P41743
PDB (SRS)1VD2    1WMH    1ZRZ    3A8W    3A8X    3ZH8   
PDB (PDBSum)1VD2    1WMH    1ZRZ    3A8W    3A8X    3ZH8   
PDB (IMB)1VD2    1WMH    1ZRZ    3A8W    3A8X    3ZH8   
PDB (RSDB)1VD2    1WMH    1ZRZ    3A8W    3A8X    3ZH8   
Human Protein AtlasENSG00000163558 [gene] [tissue] [antibody] [cell] [cancer]
Peptide AtlasP41743
HPRD02105
IPIIPI00016639   
Protein Interaction databases
DIP (DOE-UCLA)P41743
IntAct (EBI)P41743
FunCoupENSG00000163558
BioGRIDPRKCI
InParanoidP41743
Interologous Interaction database P41743
IntegromeDBPRKCI
STRING (EMBL)PRKCI
Ontologies - Pathways
Ontology : AmiGOpolarisome  Golgi membrane  protein kinase activity  protein serine/threonine kinase activity  protein serine/threonine kinase activity  protein kinase C activity  protein binding  ATP binding  phospholipid binding  nucleus  cytoplasm  endosome  cytosol  cytosol  plasma membrane  protein phosphorylation  protein targeting to membrane  cytoskeleton organization  actin filament organization  zinc ion binding  positive regulation of neuron projection development  microtubule cytoskeleton  vesicle-mediated transport  apical plasma membrane  cell migration  protein domain specific binding  cell leading edge  cellular response to insulin stimulus  cell junction assembly  negative regulation of glial cell apoptotic process  establishment of apical/basal cell polarity  intracellular signal transduction  eye photoreceptor cell development  negative regulation of apoptotic process  Schmidt-Lanterman incisure  negative regulation of neuron apoptotic process  intercellular bridge  establishment or maintenance of epithelial cell apical/basal polarity  cell-cell junction organization  cell-cell junction organization  positive regulation of glucose import  secretion  neurotrophin TRK receptor signaling pathway  Golgi vesicle budding  positive regulation of NF-kappaB transcription factor activity  positive regulation of glial cell proliferation  membrane organization  extracellular vesicular exosome  response to interleukin-1  tight junction assembly  positive regulation of establishment of protein localization to plasma membrane  positive regulation of endothelial cell apoptotic process  
Ontology : EGO-EBIpolarisome  Golgi membrane  protein kinase activity  protein serine/threonine kinase activity  protein serine/threonine kinase activity  protein kinase C activity  protein binding  ATP binding  phospholipid binding  nucleus  cytoplasm  endosome  cytosol  cytosol  plasma membrane  protein phosphorylation  protein targeting to membrane  cytoskeleton organization  actin filament organization  zinc ion binding  positive regulation of neuron projection development  microtubule cytoskeleton  vesicle-mediated transport  apical plasma membrane  cell migration  protein domain specific binding  cell leading edge  cellular response to insulin stimulus  cell junction assembly  negative regulation of glial cell apoptotic process  establishment of apical/basal cell polarity  intracellular signal transduction  eye photoreceptor cell development  negative regulation of apoptotic process  Schmidt-Lanterman incisure  negative regulation of neuron apoptotic process  intercellular bridge  establishment or maintenance of epithelial cell apical/basal polarity  cell-cell junction organization  cell-cell junction organization  positive regulation of glucose import  secretion  neurotrophin TRK receptor signaling pathway  Golgi vesicle budding  positive regulation of NF-kappaB transcription factor activity  positive regulation of glial cell proliferation  membrane organization  extracellular vesicular exosome  response to interleukin-1  tight junction assembly  positive regulation of establishment of protein localization to plasma membrane  positive regulation of endothelial cell apoptotic process  
Pathways : KEGGRap1 signaling pathway    Endocytosis    Hippo signaling pathway    Tight junction    Insulin signaling pathway   
Protein Interaction DatabasePRKCI
Wikipedia pathwaysPRKCI
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)PRKCI
snp3D : Map Gene to Disease5584
SNP (GeneSNP Utah)PRKCI
SNP : HGBasePRKCI
Genetic variants : HAPMAPPRKCI
Exome VariantPRKCI
1000_GenomesPRKCI 
ICGC programENSG00000163558 
Somatic Mutations in Cancer : COSMICPRKCI 
CONAN: Copy Number AnalysisPRKCI 
Mutations and Diseases : HGMDPRKCI
Mutations and Diseases : intOGenPRKCI
Genomic VariantsPRKCI  PRKCI [DGVbeta]
dbVarPRKCI
ClinVarPRKCI
Pred. of missensesPolyPhen-2  SIFT(SG)  SIFT(JCVI)  Align-GVGD  MutAssessor  Mutanalyser  
Pred. splicesGeneSplicer  Human Splicing Finder  MaxEntScan  
Diseases
OMIM600539   
MedgenPRKCI
GENETestsPRKCI
Disease Genetic AssociationPRKCI
Huge Navigator PRKCI [HugePedia]  PRKCI [HugeCancerGEM]
General knowledge
Homologs : HomoloGenePRKCI
Homology/Alignments : Family Browser (UCSC)PRKCI
Phylogenetic Trees/Animal Genes : TreeFamPRKCI
Chemical/Protein Interactions : CTD5584
Chemical/Pharm GKB GenePA33768
Clinical trialPRKCI
Cancer Resource (Charite)ENSG00000163558
Other databases
Probes
Litterature
PubMed167 Pubmed reference(s) in Entrez
CoreMinePRKCI
iHOPPRKCI
OncoSearchPRKCI

Bibliography

Molecular cloning and characterization of PKC iota, an atypical isoform of protein kinase C derived from insulin-secreting cells.
Selbie LA, Schmitz-Peiffer C, Sheng Y, Biden TJ.
J Biol Chem. 1993 Nov 15;268(32):24296-302.
PMID 8226978
 
Atypical protein kinase C iota protects human leukemia cells against drug-induced apoptosis.
Murray NR, Fields AP.
J Biol Chem. 1997 Oct 31;272(44):27521-4.
PMID 9346882
 
Interaction of protein kinase C zeta with ZIP, a novel protein kinase C-binding protein.
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Proc Natl Acad Sci U S A. 1997 Jun 10;94(12):6191-6.
PMID 9177193
 
Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62.
Sanchez P, De Carcer G, Sandoval IV, Moscat J, Diaz-Meco MT.
Mol Cell Biol. 1998 May;18(5):3069-80.
PMID 9566925
 
The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation.
Sanz L, Sanchez P, Lallena MJ, Diaz-Meco MT, Moscat J.
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PMID 10356400
 
Overexpression of atypical PKC in PC12 cells enhances NGF-responsiveness and survival through an NF-kappaB dependent pathway.
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PMID 10467349
 
The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42.
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Nat Cell Biol. 2000 Aug;2(8):531-9.
PMID 10934474
 
A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity.
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PMID 10873802
 
Mapping of atypical protein kinase C within the nerve growth factor signaling cascade: relationship to differentiation and survival of PC12 cells.
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PMID 10848576
 
Protein kinase C iota protects neural cells against apoptosis induced by amyloid beta-peptide.
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PMID 11042363
 
MEK5, a new target of the atypical protein kinase C isoforms in mitogenic signaling.
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PMID 11158308
 
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PMID 11260256
 
Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway.
Tisdale EJ.
J Biol Chem. 2002 Feb 1;277(5):3334-41. Epub 2001 Nov 27.
PMID 11724794
 
Phosphorylation of tyrosine 256 facilitates nuclear import of atypical protein kinase C.
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J Cell Biochem. 2002;85(1):42-53.
PMID 11891849
 
Protein kinase C isoform expression in ovarian carcinoma correlates with indicators of poor prognosis.
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Bcr-Abl regulates protein kinase Ciota (PKCiota) transcription via an Elk1 site in the PKCiota promoter.
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PMID 14670960
 
Solution structure of atypical protein kinase C PB1 domain and its mode of interaction with ZIP/p62 and MEK5.
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PMID 15143057
 
Protein kinase Ciota is required for Ras transformation and colon carcinogenesis in vivo.
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J Cell Biol. 2004 Mar 15;164(6):797-802.
PMID 15024028
 
Atypical PKCiota contributes to poor prognosis through loss of apical-basal polarity and cyclin E overexpression in ovarian cancer.
Eder AM, Sui X, Rosen DG, Nolden LK, Cheng KW, Lahad JP, Kango-Singh M, Lu KH, Warneke CL, Atkinson EN, Bedrosian I, Keyomarsi K, Kuo WL, Gray JW, Yin JC, Liu J, Halder G, Mills GB.
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PMID 16116079
 
Survival function of protein kinase C{iota} as a novel nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone-activated bad kinase.
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PMID 15705582
 
Atypical protein kinase Ciota plays a critical role in human lung cancer cell growth and tumorigenicity.
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PMID 15994303
 
Atypical protein kinase C iota is an oncogene in human non-small cell lung cancer.
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Aurothiomalate inhibits transformed growth by targeting the PB1 domain of protein kinase Ciota.
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PMID 16861740
 
Protein kinase C alpha but not PKCzeta suppresses intestinal tumor formation in ApcMin/+ mice.
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PMID 16849539
 
A novel small-molecule inhibitor of protein kinase Ciota blocks transformed growth of non-small-cell lung cancer cells.
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PMID 16452237
 
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Regulation of glioblastoma cell invasion by PKC iota and RhoB.
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PMID 18212741
 
Matrix metalloproteinase-10 is a critical effector of protein kinase Ciota-Par6alpha-mediated lung cancer.
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PMID 18427549
 
The overexpression and altered localization of the atypical protein kinase C lambda/iota in breast cancer correlates with the pathologic type of these tumors.
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Written06-2012Verline Justilien, Alan P Fields
Department of Cancer Biology, Mayo Clinic College of Medicine, Jacksonville, Florida, 32224 USA

Citation

This paper should be referenced as such :
Justilien, V ; Fields, AP
PRKCI (protein kinase C, iota)
Atlas Genet Cytogenet Oncol Haematol. 2012;16(12):913-917.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/PRKCIID41857ch3q26.html

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