Journal ArticleDOI
Protein kinase Cα (PKCα): Regulation and biological function
TLDR
Protein kinase C alpha (PKC alpha) is a serine/threonine kinase and a member of the conventional (classical) PKCs (cPKCs), which have four conserved (C1 to C4) regions.Abstract:
Protein kinase C alpha (PKC alpha) is a serine/threonine kinase and a member of the conventional (classical) PKCs (cPKCs), which have four conserved (C1 to C4) regions. This ubiquitously expressed PKC isotype is activated in response to many different kinds of stimuli and translocates from cytosol to the specialized cellular compartments (nucleus, focal adhesion, caveolae, etc.) where it is presumed to work. Therefore, PKC alpha has been implicated in a variety of cellular functions including proliferation, apoptosis, differentiation, motility, and inflammation. However, the responses induced by activation or overexpression of PKC alpha vary depending on the types, and sometimes conditions, of cells. For example, in some types of cells, PKC alpha is implicated in cell growth. In contrast, it may play a role in cell cycle arrest and differentiation in other types of cells. Therefore, alterations of cell responses induced by PKC alpha are not an intrinsic property of this isoform. The responses are modulated by dynamic interactions with cell-type specific factors: substrates, modulators and anchoring proteins.read more
Citations
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Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton.
Dos D. Sarbassov,Siraj M. Ali,Do Hyung Kim,David A. Guertin,Robert R. Latek,Hediye Erdjument-Bromage,Paul Tempst,David M. Sabatini +7 more
TL;DR: It is found that the rictor-mTOR complex modulates the phosphorylation of Protein Kinase C alpha (PKCalpha) and the actin cytoskeleton, suggesting that this aspect of TOR signaling is conserved between yeast and mammals.
Journal ArticleDOI
Toll-like receptor 2 enhances ZO-1-associated intestinal epithelial barrier integrity via protein kinase C
TL;DR: Evidence is provided that PKC is an essential component of the TLR2 signaling pathway with the physiologic consequence of directly enhancing intestinal epithelial integrity through translocation of ZO-1 on activation.
Journal ArticleDOI
Complexity of the TOR signaling network.
Ken Inoki,Kun-Liang Guan +1 more
TL;DR: New findings that have extended the complexity of TOR signaling and the different roles of the TORC complexes in yeast, flies and mammals are discussed.
Journal ArticleDOI
Characterization of the Interaction of Ingenol 3-Angelate with Protein Kinase C
Noemi Kedei,Daniel J. Lundberg,Attila Tóth,Peter Welburn,Susan H. Garfield,Peter M. Blumberg +5 more
TL;DR: I3A induced a higher level of secretion of the inflammatory cytokine interleukin 6 compared with PMA in the WEHI-231 cells and displayed a marked biphasic dose-response curve for the induction.
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Phospholipase D Signaling Pathways and Phosphatidic Acid as Therapeutic Targets in Cancer
TL;DR: This review provides a comprehensive overview of the regulation of phospholipase D activity and its modulation of cellular signaling pathways and functions, particularly in cells that are under stress conditions.
References
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Journal ArticleDOI
Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
TL;DR: It is becoming clear that agonist-induced hydrolysis of other membrane phospholipids, particularly choline phospholipsids, by phospholIPase D and phospholiptase A2 may also take part in cell signaling.
Journal ArticleDOI
Protein kinase C and lipid signaling for sustained cellular responses.
TL;DR: It is now becoming evident that stimulation of a cell surface receptor initiates a degradation cascade of various membrane lipid constituents that has potentials to induce, intensify, and prolong the activation of protein kinase C that is needed for sustained cellular responses.
Journal ArticleDOI
Protein Kinase C: Structure, Function, and Regulation
TL;DR: Multiple receptor pathways feeding into multiple lipid pathways have the common end result of activating protein kinase C by production of its second messenger, diacylglycerol.
Journal ArticleDOI
Protein kinase C alpha activates RAF-1 by direct phosphorylation
Walter Kolch,Gisela Heidecker,Georg Kochs,Richard Hummel,Haleh Vahidi,Harald Mischak,Günter Finkenzeller,Dieter Marmé,Ulf R. Rapp +8 more
TL;DR: The observation that Raf-1 and PKCα cooperate in the transformation of NIH3T3 cells is consistent with such a direct interaction, and the Ser499 phosphorylation site is necessary for this synergism.
Journal ArticleDOI
Localization of protein kinases by anchoring proteins: A theme in signal transduction
TL;DR: Data indicate that the location of these anchoring proteins provides some of the specificity of the responses mediated by each kinase and suggest that inhibitors of the interaction between the kinases and their anchoring protein may be useful as therapeutic agents.
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