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      • Record: found
      • Abstract: found
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      PKCα and PKCδ: Friends and Rivals

      review-article
      Author(s): 1 , ∗ , 2 , 1 , 2 , ∗
      Publication date (Electronic):
      Journal: The Journal of Biological Chemistry
      Publisher: American Society for Biochemistry and Molecular Biology
      Keywords: PKC, cell cycle, differentiation, apoptosis, migration, cancer, BIM, BCL-2-like protein 11, BCL-2, B cell lymphoma 2 apoptosis regulator, CDCP1, CUB domain–containing protein 1, CDK, cyclin-dependent kinase, CF, catalytic fragment, cPKC, conventional PKC, DAG, diacylglycerol, DLG, discs large MAGUK (membrane-associated guanylate kinase homologs) scaffold protein, ECM, extracellular matrix, EGFR, epidermal growth factor receptor, EMT, epithelial-to-mesenchymal transition, ER, endoplasmic reticulum, ERK, extracellular signal–regulated kinase, FGF, fibroblast growth factor, IP3, inositol 3-phosphate, MEK, mitogen-activated protein kinase kinase, MMP, matrix metalloproteinase, MSK1, mitogen- and stress-activated protein kinase 1, mTORC2, mammalian target of rapamycin complex 2, nPKC, novel PKC, NSCLC, non–small cell lung cancer, PIP2, phosphatidylinositol 4,5-bisphosphate, PP2A, protein phosphatase 2A, PTB, phosphotyrosine-binding motif, ROS, reactive oxygen species, RTK, receptor tyrosine kinase, TKI, tyrosine kinase inhibitor, TNF, tumor necrosis factor, ZEB, zinc finger E-box-binding homeobox

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          Abstract

          PKC comprises a large family of serine/threonine kinases that share a requirement for allosteric activation by lipids. While PKC isoforms have significant homology, functional divergence is evident among subfamilies and between individual PKC isoforms within a subfamily. Here, we highlight these differences by comparing the regulation and function of representative PKC isoforms from the conventional (PKCα) and novel (PKCδ) subfamilies. We discuss how unique structural features of PKCα and PKCδ underlie differences in activation and highlight the similar, divergent, and even opposing biological functions of these kinases. We also consider how PKCα and PKCδ can contribute to pathophysiological conditions and discuss challenges to targeting these kinases therapeutically.

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          Most cited references385

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          The extended protein kinase C superfamily.

          H Mellor, P J Parker (1998)
          Members of the mammalian protein kinase C (PKC) superfamily play key regulatory roles in a multitude of cellular processes, ranging from control of fundamental cell autonomous activities, such as proliferation, to more organismal functions, such as memory. However, understanding of mammalian PKC signalling systems is complicated by the large number of family members. Significant progress has been made through studies based on comparative analysis, which have defined a number of regulatory elements in PKCs which confer specific location and activation signals to each isotype. Further studies on simple organisms have shown that PKC signalling paradigms are conserved through evolution from yeast to humans, underscoring the importance of this family in cellular signalling and giving novel insights into PKC function in complex mammalian systems.
          Article 0 comments Cited 176 times – based on 0 reviews     Review now
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            ERK and cell death: mechanisms of ERK-induced cell death--apoptosis, autophagy and senescence.

            Jean-Claude Chambard, Sébastien Cagnol (2009)
            The Ras/Raf/extracellular signal-regulated kinase (ERK) signaling pathway plays a crucial role in almost all cell functions and therefore requires exquisite control of its spatiotemporal activity. Depending on the cell type and stimulus, ERK activity will mediate different antiproliferative events, such as apoptosis, autophagy and senescence in vitro and in vivo. ERK activity can promote either intrinsic or extrinsic apoptotic pathways by induction of mitochondrial cytochrome c release or caspase-8 activation, permanent cell cycle arrest or autophagic vacuolization. These unusual effects require sustained ERK activity in specific subcellular compartments and could depend on the presence of reactive oxygen species. We will summarize the mechanisms involved in Ras/Raf/ERK antiproliferative functions.
            Article 0 comments Cited 168 times – based on 0 reviews     Review now
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              Mitogenic signalling and the p16INK4a-Rb pathway cooperate to enforce irreversible cellular senescence.

              Hideyuki Saya, Keiichi Nakayama, Kimi Yamakoshi … (2006)
              The p16(INK4a) cyclin-dependent kinase inhibitor has a key role in establishing stable G1 cell-cycle arrest through activating the retinoblastoma (Rb) tumour suppressor protein pRb in cellular senescence. Here, we show that the p16(INK4a) /Rb-pathway also cooperates with mitogenic signals to induce elevated intracellular levels of reactive oxygen species (ROS), thereby activating protein kinase Cdelta (PKCdelta) in human senescent cells. Importantly, once activated by ROS, PKCdelta promotes further generation of ROS, thus establishing a positive feedback loop to sustain ROS-PKCdelta signalling. Sustained activation of ROS-PKCdelta signalling irreversibly blocks cytokinesis, at least partly through reducing the level of WARTS (also known as LATS1), a mitotic exit network (MEN) kinase required for cytokinesis, in human senescent cells. This irreversible cytokinetic block is likely to act as a second barrier to cellular immortalization ensuring stable cell-cycle arrest in human senescent cells. These results uncover an unexpected role for the p16(INK4a)-Rb pathway and provide a new insight into how senescent cell-cycle arrest is enforced in human cells.
              Article 0 comments Cited 159 times – based on 0 reviews     Review now
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                Author and article information

                Contributors
                Jennifer D. Black
                Mary E. Reyland
                Journal
                Journal ID (nlm-ta): J Biol Chem
                Journal ID (iso-abbrev): J Biol Chem
                Title: The Journal of Biological Chemistry
                Publisher: American Society for Biochemistry and Molecular Biology
                ISSN (Print): 0021-9258
                ISSN (Electronic): 1083-351X
                Publication date PMC-release: 24 June 2022
                Publication date Collection: August 2022
                Publication date (Electronic): 24 June 2022
                Volume: 298
                Issue: 8
                Electronic Location Identifier: 102194
                Affiliations
                [1 ]Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska, USA
                [2 ]Department of Craniofacial Biology, School of Dental Medicine, University of Colorado Anschutz Medical Campus, Aurora, Colorado, USA
                Author notes
                [∗ ]For correspondence: Mary E. Reyland; Jennifer D. Black Jennifer.Black@ 123456unmc.edu Mary.Reyland@ 123456cuanschutz.edu
                Article
                Publisher Item ID: S0021-9258(22)00636-6 Publisher ID: 102194
                DOI: 10.1016/j.jbc.2022.102194
                PMC ID: 9352922
                PubMed ID: 35760100
                SO-VID: d13d8bb0-ce86-4b97-8a02-fd64bba269a2
                Copyright © © 2022 The Authors
                License:

                This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

                History
                Date received : 10 March 2022
                Date revision received : 13 June 2022
                Categories
                Subject: JBC Reviews

                ScienceOpen disciplines: Biochemistry
                Keywords: pkc,cell cycle,differentiation,apoptosis,migration,cancer,bim, bcl-2-like protein 11,bcl-2, b cell lymphoma 2 apoptosis regulator,cdcp1, cub domain–containing protein 1,cdk, cyclin-dependent kinase,cf, catalytic fragment,cpkc, conventional pkc,dag, diacylglycerol,dlg, discs large maguk (membrane-associated guanylate kinase homologs) scaffold protein,ecm, extracellular matrix,egfr, epidermal growth factor receptor,emt, epithelial-to-mesenchymal transition,er, endoplasmic reticulum,erk, extracellular signal–regulated kinase,fgf, fibroblast growth factor,ip3, inositol 3-phosphate,mek, mitogen-activated protein kinase kinase,mmp, matrix metalloproteinase,msk1, mitogen- and stress-activated protein kinase 1,mtorc2, mammalian target of rapamycin complex 2,npkc, novel pkc,nsclc, non–small cell lung cancer,pip2, phosphatidylinositol 4,5-bisphosphate,pp2a, protein phosphatase 2a,ptb, phosphotyrosine-binding motif,ros, reactive oxygen species,rtk, receptor tyrosine kinase,tki, tyrosine kinase inhibitor,tnf, tumor necrosis factor,zeb, zinc finger e-box-binding homeobox
                Data availability:
                ScienceOpen disciplines: Biochemistry
                Keywords: pkc, cell cycle, differentiation, apoptosis, migration, cancer, bim, bcl-2-like protein 11, bcl-2, b cell lymphoma 2 apoptosis regulator, cdcp1, cub domain–containing protein 1, cdk, cyclin-dependent kinase, cf, catalytic fragment, cpkc, conventional pkc, dag, diacylglycerol, dlg, discs large maguk (membrane-associated guanylate kinase homologs) scaffold protein, ecm, extracellular matrix, egfr, epidermal growth factor receptor, emt, epithelial-to-mesenchymal transition, er, endoplasmic reticulum, erk, extracellular signal–regulated kinase, fgf, fibroblast growth factor, ip3, inositol 3-phosphate, mek, mitogen-activated protein kinase kinase, mmp, matrix metalloproteinase, msk1, mitogen- and stress-activated protein kinase 1, mtorc2, mammalian target of rapamycin complex 2, npkc, novel pkc, nsclc, non–small cell lung cancer, pip2, phosphatidylinositol 4,5-bisphosphate, pp2a, protein phosphatase 2a, ptb, phosphotyrosine-binding motif, ros, reactive oxygen species, rtk, receptor tyrosine kinase, tki, tyrosine kinase inhibitor, tnf, tumor necrosis factor, zeb, zinc finger e-box-binding homeobox

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