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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Protein kinase C, zeta

PKCzeta, protein kinase C zeta
Protein kinase C (PKC) zeta is a member of the PKC family of serine/threonine kinases which are involved in a variety of cellular processes such as proliferation, differentiation and secretion. Unlike the classical PKC isoenzymes which are calcium-dependent, PKC zeta exhibits a kinase activity which is independent of calcium and diacylglycerol but not of phosphatidylserine. Furthermore, it is insensitive to typical PKC inhibitors and cannot be activated by phorbol ester. Unlike the classical PKC isoenzymes, it has only a single zinc finger module. These structural and biochemical properties indicate that the zeta subspecies is related to, but distinct from other isoenzymes of PKC. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Protein Kinase C-alpha, V1a, Insulin, Akt, CAN
Papers using PKCzeta antibodies
Insulin-like growth factor-I inhibits transcriptional responses of transforming growth factor-beta by phosphatidylinositol 3-kinase/Akt-dependent suppression of the activation of Smad3 but not Smad2.
Nurminsky Dmitry I., In PLoS ONE, 2002
... EGFR, (Santacruz, sc 03, 1005), Glucose-6-P dehydrogenase (Abcam, ab34436), Protein Kinase C-zeta (Cell signaling, ab51157), P-PKC-zeta (Abcam, ab76129), Syntaxin 4 (Abcam, ab57841), ...
Papers on PKCzeta
The memory-enhancing effect of erucic acid on scopolamine-induced cognitive impairment in mice.
Ryu et al., Seoul, South Korea. In Pharmacol Biochem Behav, Feb 2016
The administration of erucic acid increased the phosphorylation levels of phosphatidylinositide 3-kinase (PI3K), protein kinase C zeta (PKCζ), extracellular signal-regulated kinase (ERK), cAMP response element-binding protein (CREB) and additional protein kinase B (Akt) in the hippocampus.
NUMB phosphorylation destabilizes p53 and promotes self-renewal of tumor-initiating cells by a NANOG-dependent mechanism in liver cancer.
Machida et al., Okayama, Japan. In Hepatology, Nov 2015
NANOG phosphorylates NUMB by atypical protein kinase C zeta (aPKCζ), through the direct induction of Aurora A kinase (AURKA) and the repression of an aPKCζ inhibitor, lethal (2) giant larvae.
Angiotensin IV possibly acts through PKMzeta in the hippocampus to regulate cognitive memory in rats.
Huang et al., Taipei, Taiwan. In Neuropeptides, Oct 2015
PKMzeta was identified to be a fragment of PKCzeta (protein kinase Czeta).
IGFBP-3 reduces eNOS and PKCzeta phosphorylation, leading to lowered VEGF levels.
Steinle et al., Memphis, United States. In Mol Vis, 2014
METHODS: To test this hypothesis, we grew primary human retinal endothelial cells in normal glucose (5 mM) or high glucose (25 mM) for three days, treated with IGFBP-3 NB plasmid (a plasmid of IGFBP-3 that cannot bind IGF-1), followed by western blotting for eNOS, protein kinase C zeta (PKCzeta), and VEGF.
PKCζ Promotes Breast Cancer Invasion by Regulating Expression of E-cadherin and Zonula Occludens-1 (ZO-1) via NFκB-p65.
Paul et al., Kansas City, United States. In Sci Rep, 2014
Atypical Protein Kinase C zeta (PKCζ) forms Partitioning-defective (PAR) polarity complex for apico-basal distribution of membrane proteins essential to maintain normal cellular junctional complexes and tissue homeostasis.
Protein kinase C isoforms have differential roles in the regulation of human sebocyte biology.
Bíró et al., Debrecen, Hungary. In J Invest Dermatol, 2012
SZ95 sebocytes express the conventional cPKCalpha; the novel nPKCdelta, epsilon, and eta; and the atypical aPKCzeta
High mobility group box-1 is phosphorylated by protein kinase C zeta and secreted in colon cancer cells.
Kim et al., Seoul, South Korea. In Biochem Biophys Res Commun, 2012
these findings suggest that PKC-zeta is involved in the phosphorylation of HMGB1, and the phosphorylation of specific serine residues in the nuclear localization signal regions is related to enhanced HMGB1 secretion in colon cancer cells.
Splice variant PRKC-ζ(-PrC) is a novel biomarker of human prostate cancer.
Foster et al., Liverpool, United Kingdom. In Br J Cancer, 2012
A novel sequence was identified within the 3'-terminal domain of human PRKCZ.
Activation of Stat3 in endothelial cells following hypoxia-reoxygenation is mediated by Rac1 and protein Kinase C.
Becker et al., Baltimore, United States. In Biochim Biophys Acta, 2012
Stat3 forms a multiprotein complex with Rac1 and PKC in an hypoxia-reoxygenation-dependent manner.
Down-regulation of PKCζ in renal cell carcinoma and its clinicopathological implications.
Hour et al., Taipei, Taiwan. In J Biomed Sci, 2011
Protein kinase C (PKC) zeta expression was significantly higher in normal than in cancerous tissues. Similarly, PKC zeta expression was down-regulated in four renal cancer cell lines compared to immortalized benign renal tubular cells.
PKCzeta-regulated inflammation in the nonhematopoietic compartment is critical for obesity-induced glucose intolerance.
Moscat et al., Cincinnati, United States. In Cell Metab, 2010
PKCzeta as a critical negative regulator of IL-6 in the control of obesity-induced inflammation in adipocytes.
Participation of signaling pathways in the derepression of luteinizing hormone receptor transcription.
Zhang et al., Bethesda, United States. In Mol Cell Endocrinol, 2010
The HDAC inhibitor TSA-induced cell-specific phosphatase release from the promoter, which serves as an 'on' mechanism for Sp1 phosphorylation by phosphatidylinositol 3-kinase/protein kinase Czeta (PI3K/PKCzeta) at Ser641, leading to p107 repressor derecruitment and LHR transcriptional activation.
Ceramide in stress response.
Rozenova et al., Lexington, United States. In Adv Exp Med Biol, 2009
The latter summarizes the mechanisms by which ceramide activate its direct targets, PKCzeta, PP2A and cathepsin D. The ability of ceramide to affect membrane organization is discussed in the light of its relevance to cell signaling.
Of the atypical PKCs, Par-4 and p62: recent understandings of the biology and pathology of a PB1-dominated complex.
Wooten et al., Cincinnati, United States. In Cell Death Differ, 2009
The role that PKCzeta, PKClambda/iota, and Par-4 have in lung and prostate cancer in vivo and in humans will be extensively covered in this article, as will the multifunctional role of p62 as a novel hub in cell signaling during cancer and inflammation, and the mechanistic details and controversial data published on its potential role in aggregate formation and signaling.
Aurora A moonlights in neurite extension.
Gleeson et al., In Nat Cell Biol, 2009
PKCzeta activates Aurora A, which in turn phosphorylates NDEL1 to promote neurite extension.
Meningococcal type IV pili recruit the polarity complex to cross the brain endothelium.
Nassif et al., Paris, France. In Science, 2009
Here, type IV pili-mediated adhesion of N. meningitidis to human brain endothelial cells was found to recruit the Par3/Par6/PKCzeta polarity complex that plays a pivotal role in the establishment of eukaryotic cell polarity and the formation of intercellular junctions.
Protein kinase C isoforms: Multi-functional regulators of cell life and death.
Reyland, Aurora, United States. In Front Biosci, 2008
These studies suggest that PKC-alpha, PKC-epsilon, and the atypical PKC's, PKC-lambda/iota and PKC-zeta, preferentially function to promote cell proliferation and survival, while the novel isoform, PKC-delta is an important regulator of apoptosis.
PKMzeta, LTP maintenance, and the dynamic molecular biology of memory storage.
Sacktor, United States. In Prog Brain Res, 2007
Although full-length PKC isoforms respond to transient second messengers, and are involved in LTP induction, PKMzeta is a second messenger-independent kinase, consisting of the independent catalytic domain of PKCzeta, and is persistently active to sustain LTP maintenance.
Nuclear movement regulated by Cdc42, MRCK, myosin, and actin flow establishes MTOC polarization in migrating cells.
Gundersen et al., New York City, United States. In Cell, 2005
Nuclear movement was unaffected by the inhibition of dynein, Par6, or PKCzeta, yet these components were essential for MTOC reorientation, as they maintained the MTOC at the cell centroid.
Regulation of cell polarity and protrusion formation by targeting RhoA for degradation.
Wrana et al., Toronto, Canada. In Science, 2004
Atypical protein kinase C zeta (PKCzeta), an effector of the Cdc42/Rac1-PAR6 polarity complex, recruited Smurf1 to cellular protrusions, where it controlled the local level of RhoA.
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