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      A cancer-associated, genome protective programme engaging PKCε

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          Abstract

          Associated with their roles as targets for tumour promoters, there has been a long-standing interest in how members of the protein kinase C (PKC) family act to modulate cell growth and division. This has generated a great deal of observational data, but has for the most part not afforded clear mechanistic insights into the control mechanisms at play. Here, we review the roles of PKCε in protecting transformed cells from non-disjunction. In this particular cell cycle context, there is a growing understanding of the pathways involved, affording biomarker and interventional insights and opportunities.

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          Aurora B-mediated abscission checkpoint protects against tetraploidization.

          Patrick Steigemann, Claudia Wurzenberger, Michael Schmitz … (2009)
          Genomic abnormalities are often seen in tumor cells, and tetraploidization, which results from failures during cytokinesis, is presumed to be an early step in cancer formation. Here, we report a cell division control mechanism that prevents tetraploidization in human cells with perturbed chromosome segregation. First, we found that Aurora B inactivation promotes completion of cytokinesis by abscission. Chromosome bridges sustained Aurora B activity to posttelophase stages and thereby delayed abscission at stabilized intercellular canals. This was essential to suppress tetraploidization by furrow regression in a pathway further involving the phosphorylation of mitotic kinesin-like protein 1 (Mklp1). We propose that Aurora B is part of a sensor that responds to unsegregated chromatin at the cleavage site. Our study provides evidence that in human cells abscission is coordinated with the completion of chromosome segregation to protect against tetraploidization by furrow regression.
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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.
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              Protein kinase C: poised to signal.

              Alexandra C Newton (2010)
              Nestled at the tip of a branch of the kinome, protein kinase C (PKC) family members are poised to transduce signals emanating from the cell surface. Cell membranes provide the platform for PKC function, supporting the maturation of PKC through phosphorylation, its allosteric activation by binding specific lipids, and, ultimately, promoting the downregulation of the enzyme. These regulatory mechanisms precisely control the level of signaling-competent PKC in the cell. Disruption of this regulation results in pathophysiological states, most notably cancer, where PKC levels are often grossly altered. This review introduces the PKC family and then focuses on recent advances in understanding the cellular regulation of its diacylglycerol-regulated members.
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                Author and article information

                Contributors
                Peter J. Parker
                Journal
                Journal ID (nlm-ta): Adv Biol Regul
                Journal ID (iso-abbrev): Adv Biol Regul
                Title: Advances in Biological Regulation
                Publisher: Elsevier
                ISSN (Print): 2212-4926
                ISSN (Electronic): 2212-4934
                Publication date PMC-release: 1 December 2020
                Publication date (Print): December 2020
                Volume: 78
                Electronic Location Identifier: 100759
                Affiliations
                [a ]Protein Phosphorylation Laboratory, Francis Crick Institute, London, NW1 1AT, UK
                [b ]School of Cancer and Pharmaceutical Sciences, Guy's Campus, London, SE1 1UL, UK
                [c ]Cancer Research UK, Manchester Institute, Alderley Park, SK10 4TG, UK
                [d ]Barts Cancer Institute, Charterhouse Square, London, EC1M 6BE, UK
                [e ]GSK, Stevenage, Hertfordshire, SG1 2NY, UK
                [f ]Department of Medicine and Surgery, University of Parma, Parma, Italy
                Author notes
                [∗ ]Corresponding author. Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK. peter.parker@ 123456crick.ac.uk
                Article
                Publisher Item ID: S2212-4926(20)30070-1 Publisher ID: 100759
                DOI: 10.1016/j.jbior.2020.100759
                PMC ID: 7689578
                PubMed ID: 33039823
                SO-VID: 47cecdb8-caa0-4d65-b822-c4516f264bdc
                Copyright © © 2020 The Authors
                License:

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

                History
                Date received : 14 September 2020
                Date revision received : 27 September 2020
                Date accepted : 2 October 2020
                Categories
                Subject: Article

                Keywords: pkce,cell cycle,non-disjunction,aurora b
                Data availability:
                Keywords: pkce, cell cycle, non-disjunction, aurora b

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