ArticleThe Biochemical journal2004
Molecular mechanisms regulating protein kinase Czeta turnover and cellular transformation.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 31 citations in OpenAlex.
- Novel components in the nuclear factor-kappa B (NF-κB) signaling pathways of endothelial cells under hyperglycemic-ischemic conditions.Frontiers in cardiovascular medicine · 2024Article
- Attenuation of amyloid-β generation by atypical protein kinase C-mediated phosphorylation of engulfment adaptor PTB domain containing 1 threonine 35.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- aPKC: the Kinase that Phosphorylates Cell Polarity.F1000Research · 2018Review
- Atypical PKCs in memory maintenance: the roles of feedback and redundancy.Learning & memory (Cold Spring Harbor, N.Y.) · 2015Article
- Article
- Splice variant PRKC-ζ(-PrC) is a novel biomarker of human prostate cancer.British journal of cancer · 2012Article
- PDK1 in apical signaling endosomes participates in the rescue of the polarity complex atypical PKC by intermediate filaments in intestinal epithelia.Molecular biology of the cell · 2012Article
- The protein kinase Mζ network as a bistable switch to store neuronal memory.BMC systems biology · 2010Article
- Interplay between REST and nucleolin transcription factors: a key mechanism in the overexpression of genes upon increased phosphorylation.Nucleic acids research · 2010Article
- Atypical protein kinase C activity is required for extracellular matrix degradation and invasion by Src-transformed cells.Journal of cellular physiology · 2009Article
- Alpha1-AMP-activated protein kinase regulates hypoxia-induced Na,K-ATPase endocytosis via direct phosphorylation of protein kinase C zeta.Molecular and cellular biology · 2009Article
- Protein kinase C family: on the crossroads of cell signaling in skin and tumor epithelium.Journal of cancer research and clinical oncology · 2007Review
- Regulation of protein kinase Mzeta synthesis by multiple kinases in long-term potentiation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
- Endothelial protein kinase C isoform identity and differential activity of PKCzeta in an athero-susceptible region of porcine aorta.Circulation research · 2005Article
- Protein kinase Czeta regulates phospholipase D activity in rat-1 fibroblasts expressing the alpha1A adrenergic receptor.BMC cell biology · 2004Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The regulation of protein kinase C (PKC)zeta in relation to its turnover, cell growth and transformation was investigated in Rat2 fibroblasts by over-expressing wild-type or mutant forms of PKCzeta. Deletion of the pseudosubstrate site (PSS) produced the most active mutant (PKCzeta Delta PSS), but mutants designed to mimic phosphorylated PKCzeta had lower specific activities in an in vitro assay. The mutant lacking phosphorylation at the Thr-560 site (T560A) had similar specific activity to wild-type PKCzeta. The T560A mutant also protected PKCzeta against proteolysis, whereas phosphorylation at Thr-410 targeted it towards proteosomal degradation. Blocking proteosomal degradation with lactacystin caused the accumulation of full-length PKCzeta Delta PSS, T410E, PKCzeta Delta PSS T410/560E, PKCzeta and T560A. Expressed PKCzeta activity was paralleled by extracellular-regulated protein kinase activation, increased cell division, serum-independent growth and focus formation. These foci were seen for cells expressing higher PKCzeta activity (PKCzeta Delta PSS, PKCzeta Delta PSS T410/560E and T560A mutants), but these fibroblasts did not show significant anchorage-independent growth. This work provides novel information concerning the role of the PSS and phosphorylation sites in regulating the activity and turnover of an atypical PKC and shows how this activity can induce cell transformation with respect to focus formation.
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