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Protein kinase C, iota

PKClambda, PKCI, protein kinase Ciota, protein kinase C lambda
This gene encodes a member of the protein kinase C (PKC) family of serine/threonine protein kinases. The PKC family comprises at least eight members, which are differentially expressed and are involved in a wide variety of cellular processes. This protein kinase is calcium-independent and phospholipid-dependent. It is not activated by phorbolesters or diacylglycerol. This kinase can be recruited to vesicle tubular clusters (VTCs) by direct interaction with the small GTPase RAB2, where this kinase phosphorylates glyceraldehyde-3-phosphate dehydrogenase (GAPD/GAPDH) and plays a role in microtubule dynamics in the early secretory pathway. This kinase is found to be necessary for BCL-ABL-mediated resistance to drug-induced apoptosis and therefore protects leukemia cells against drug-induced apoptosis. There is a single exon pseudogene mapped on chromosome X. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Insulin, PKCzeta, HAD, V1a, ACID
Papers on PKClambda
5-Aminoimidazole-4-carboxyamide-1-β-D-ribofranoside stimulates the rat enhancer of split- and hairy-related protein-2 gene via atypical protein kinase C lambda.
Yamada et al., Matsumoto, Japan. In J Biochem, Dec 2015
Western blot analyses showed that AICAR rapidly activated atypical PKC lambda (aPKCλ).
Regulation of mitochondrial function and cellular energy metabolism by protein kinase C-λ/ι: a novel mode of balancing pluripotency.
Paul et al., Kansas City, United States. In Stem Cells, 2014
Here, using murine embryonic stem cells (ESCs) as a model system, we demonstrate that atypical protein kinase C isoform, PKC lambda/iota (PKCλ/ι), is a key regulator of mitochondrial function in ESCs.
Insulin stimulates the expression of the SHARP-1 gene via multiple signaling pathways.
Yamada et al., Matsumoto, Japan. In Horm Metab Res, 2014
In fact, overexpression of a dominant negative form of atypical protein kinase C lambda (aPKCλ) significantly decreased the induction of the SHARP-1 mRNA.
Protein kinase C inhibitor generates stable human tolerogenic dendritic cells.
Yasukawa et al., Japan. In J Immunol, 2013
PKCI-treated human DCs were generated by subjecting them to a maturation process after differentiation of immature DCs.
Localization of aPKC lambda/iota and its interacting protein, Lgl2, is significantly associated with lung adenocarcinoma progression.
Iwazaki et al., In Tokai J Exp Clin Med, 2012
Atypical protein kinase C lambda/iota (aPKC λ/ι) is expressed in several human cancers; however, the correlation between aPKC λ/ι localization and cancer progression in human lung adenocarcinoma (LAC) remains to be clarified.
Role of adipose and hepatic atypical protein kinase C lambda (PKCλ) in the development of obesity and glucose intolerance.
Hofmann et al., Cincinnati, United States. In Adipocyte, 2012
PKCλ, an atypical member of the multifunctional protein kinase C family, has been implicated in the regulation of insulin-stimulated glucose transport and of the intracellular immune response.
(-)-Epigallocatechin-3-gallate stimulates both AMP-activated protein kinase and nuclear factor-kappa B signaling pathways.
Yamada et al., Matsumoto, Japan. In Food Chem, 2012
We previously reported that (-)-epigallocatechin-3-gallate (EGCG) increased the level of SHARP-1 mRNA via a phosphoinositide 3-kinase/atypical protein kinase C lambda signaling pathway in rat H4IIE hepatoma cells.
Repression of cancer cell senescence by PKCι.
Lorimer et al., Ottawa, Canada. In Oncogene, 2012
It was concluded that protein kinase C iota is overexpressed in a subset of cancers where the enzyme functions to suppress premature senescence. This function appears to be restricted to cancer cells.
The Proto-oncogene PKCι regulates the alternative splicing of Bcl-x pre-mRNA.
Chalfant et al., Richmond, United States. In Mol Cancer Res, 2012
In summary, the PI3K/PKCiota regulates the alternative splicing of Bcl-x pre-mRNA with implications in the cell survival of NSCLC cells.
Regulation of Cdk7 activity through a phosphatidylinositol (3)-kinase/PKC-ι-mediated signaling cascade in glioblastoma.
Acevedo-Duncan et al., Tampa, United States. In Carcinogenesis, 2012
glioma cells may be proliferating through a novel PI (3)-kinase-/PKC-iota/Cdk7/cdk2-mediated pathway.
Protein kinase C iota regulates pancreatic acinar-to-ductal metaplasia.
Murray et al., Jacksonville, United States. In Plos One, 2011
PKCiota is an early marker of pancreatic neoplasia and PKCiota is a potential downstream target of K-ras(G12D) in pancreatic ductal metaplasia in vivo.
Hydrogen sulfide and L-cysteine increase phosphatidylinositol 3,4,5-trisphosphate (PIP3) and glucose utilization by inhibiting phosphatase and tensin homolog (PTEN) protein and activating phosphoinositide 3-kinase (PI3K)/serine/threonine protein kinase (AKT)/protein kinase Cζ/λ (PKCζ/λ) in 3T3l1 adipocytes.
Jain et al., Shreveport, United States. In J Biol Chem, 2011
Hydrogen sulfide and L-cysteine increase phosphatidylinositol 3,4,5-trisphosphate and glucose utilization by inhibiting PTEN protein and activating PI3K,AKT, PKCzeta/lambda in 3T3l1 adipocytes.
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 recent identification of a novel protein-protein interaction module, termed PB1, in critical signaling molecules such as p62 (also known as sequestosome1), the atypical PKCs, and Par-6, has unveiled the existence of a new set of signaling complexes, which can be central to several biological processes from development to cancer.
Protein kinase C isoforms: Multi-functional regulators of cell life and death.
Reyland, Aurora, United States. In Front Biosci, 2008
While early studies relied on broad spectrum chemical activators or inhibitors of this family, the generation of isoform specific tools has greatly facilitated our understanding of the contribution of specific PKC isoforms to cell proliferation and apoptosis.
Targeting the oncogenic protein kinase Ciota signalling pathway for the treatment of cancer.
Regala et al., Jacksonville, United States. In Biochem Soc Trans, 2007
To date, however, only one PKC isoenzyme, the aPKC [atypical PKCiota (protein kinase Ciota)], has been identified as a human oncogene [Regala, Weems, Jamieson, Khoor, Edell, Lohse and Fields (2005) Cancer Res.
Divergent regulation of hepatic glucose and lipid metabolism by phosphoinositide 3-kinase via Akt and PKClambda/zeta.
Kahn et al., Boston, United States. In Cell Metab, 2006
L-p85DKO mice failed to activate PI3K or generate PIP(3) upon insulin stimulation or activate its two major effectors, Akt and PKClambda/xi.
Essential role of Src-family protein tyrosine kinases in NF-kappaB activation during B cell development.
Tarakhovsky et al., New York City, United States. In Nat Immunol, 2003
Impaired NF-kappaB induction was overcome by the activation of protein kinase C (PKC)-lambda, thus suggesting the involvement of PKC-lambda in pre-BCR-mediated SFK-dependent activation of NF-kappaB.
Protein kinase C lambda/iota (PKClambda/iota): a PKC isotype essential for the development of multicellular organisms.
Ohno et al., Yokohama, Japan. In J Biochem, 2003
PKClambda/iota belongs to the third group of the PKC family, atypical PKC (aPKC), together with PKCzeta based on its sequence divergence from conventional and novel PKCs observed not only in the N-terminal regulatory domain but also in the kinase domain.
The function of MITF and associated proteins in mast cells.
Razin et al., Jerusalem, Israel. In Mol Immunol, 2002
A search for MITF-associated proteins, using a mast cell library that was screened with a construct that encodes the basic helix-loop-helix leucine zipper (bHLH-Zip) domain of MITF, resulted in the isolation of the protein kinase C interacting (PKCI) protein 1 and protein inhibitor of activated STAT3 (PIAS3).
Structure-based analysis of catalysis and substrate definition in the HIT protein family.
Hendrickson et al., New York City, United States. In Science, 1997
The histidine triad (HIT) protein family is among the most ubiquitous and highly conserved in nature, but a biological activity has not yet been identified for any member of the HIT family.
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