ArticleMolecular and cellular biology1997
Positioning atypical protein kinase C isoforms in the UV-induced apoptotic signaling cascade.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 167 citations in OpenAlex.
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- Apoptosis by [Pt(O,O'-acac)(γ-acac)(DMS)] requires PKC-δ mediated p53 activation in malignant pleural mesothelioma.PloS one · 2017Article
- The tumor suppressor prostate apoptosis response-4 (Par-4) is regulated by mutant IDH1 and kills glioma stem cells.Acta neuropathologica · 2014Article
- Par6B and atypical PKC regulate mitotic spindle orientation during epithelial morphogenesis.The Journal of biological chemistry · 2011Article
- Nutraceutical antioxidants as novel neuroprotective agents.Molecules (Basel, Switzerland) · 2010Review
- Interplay between REST and nucleolin transcription factors: a key mechanism in the overexpression of genes upon increased phosphorylation.Nucleic acids research · 2010Article
- Protein kinase C isoforms: Multi-functional regulators of cell life and death.Frontiers in bioscience (Landmark edition) · 2009Review
- Apoptosis and tumor resistance conferred by Par-4.Cancer biology & therapy · 2008Review
- Human DNA polymerase eta activity and translocation is regulated by phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Simultaneous manipulation of multiple brain targets by green tea catechins: a potential neuroprotective strategy for Alzheimer and Parkinson diseases.CNS neuroscience & therapeutics · 2008Review
- Delayed Cell Cycle Progression and Apoptosis Induced by Hemicellulase-Treated Agaricus blazei.Evidence-based complementary and alternative medicine : eCAM · 2007Article
- Protection of glioblastoma cells from cisplatin cytotoxicity via protein kinase Ciota-mediated attenuation of p38 MAP kinase signaling.Oncogene · 2006Article
- Regulation of caspase 9 through phosphorylation by protein kinase C zeta in response to hyperosmotic stress.Molecular and cellular biology · 2005Article
- Cooperation of amphiregulin and insulin-like growth factor-1 inhibits Bax- and Bad-mediated apoptosis via a protein kinase C-dependent pathway in non-small cell lung cancer cells.The Journal of biological chemistry · 2005Article
- Molecular mechanisms regulating protein kinase Czeta turnover and cellular transformation.The Biochemical journal · 2004Article
- Identification of a unique core domain of par-4 sufficient for selective apoptosis induction in cancer cells.Molecular and cellular biology · 2003Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent studies have documented the involvement of the atypical protein kinase C (aPKC) isoforms in important cellular functions such as cell proliferation and survival. Exposure of cells to a genotoxic stimulus that induces apoptosis, such as UV irradiation, leads to a profound inhibition of the atypical PKC activity in vivo. In this study, we addressed the relationship between this phenomenon and different proteins involved in the apoptotic response. We show that (i) the inhibition of the aPKC activity precedes UV-induced apoptosis; (ii) UV-induced aPKC inhibition and apoptosis are independent of p53; (iii) Bcl-2 proteins are potent modulators of aPKC activity; and (iv) the aPKCs are located upstream of the interleukin-converting enzyme-like protease system, which is required for the induction of apoptosis by both Par-4 (a selective aPKC inhibitor) and UV irradiation. We also demonstrate here that inhibition of aPKC activity leads to a decrease in mitogen-activated protein (MAP) kinase activity and simultaneously an increase in p38 activity. Both effects are critical for the induction of apoptosis in response to Par-4 expression and UV irradiation. Collectively, these results clarify the position of the aPKCs in the UV-induced apoptotic pathway and strongly suggest that MAP kinases play a role in this signaling cascade.
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