ArticleProceedings of the National Academy of Sciences of the United States of America1995
Protein kinase C epsilon is localized to the Golgi via its zinc-finger domain and modulates Golgi function.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
35 citing papers in PubMed, 136 citations in OpenAlex.
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- V-ATPase V0a1 promotes Weibel-Palade body biogenesis through the regulation of membrane fission.eLife · 2021Article
- Mechanisms of Insulin Action and Insulin Resistance.Physiological reviews · 2018Review
- Evolving mechanisms of vascular smooth muscle contraction highlight key targets in vascular disease.Biochemical pharmacology · 2018Review
- Clinical value of miR-182-5p in lung squamous cell carcinoma: a study combining data from TCGA, GEO, and RT-qPCR validation.World journal of surgical oncology · 2018Article
- Quantifying lipid changes in various membrane compartments using lipid binding protein domains.Cell calcium · 2017Review
- Protein Kinase C as Regulator of Vascular Smooth Muscle Function and Potential Target in Vascular Disorders.Advances in pharmacology (San Diego, Calif.) · 2017Review
- Article
- p23/Tmp21 differentially targets the Rac-GAP beta2-chimaerin and protein kinase C via their C1 domains.Molecular biology of the cell · 2010Article
- Nociceptor subpopulations involved in hyperalgesic priming.Neuroscience · 2010Article
- Specific subcellular targeting of PKCalpha and PKCepsilon in normal and tumoral lactotroph cells by PMA-mitogenic stimulus.Journal of molecular histology · 2009Article
- Phosphoinositide signaling: new tools and insights.Physiology (Bethesda, Md.) · 2009Review
- A 20-amino acid module of protein kinase C{epsilon} involved in translocation and selective targeting at cell-cell contacts.The Journal of biological chemistry · 2009Article
- Structural basis of protein kinase C isoform function.Physiological reviews · 2008Review
- Differential recruitment of PKC isoforms in HeLa cells during redox stress.Cell stress & chaperones · 2007Article
- Specific and nonspecific membrane-binding determinants cooperate in targeting phosphatidylinositol transfer protein beta-isoform to the mammalian trans-Golgi network.Molecular biology of the cell · 2006Article
- PKCeta is required for beta1gamma2/beta3gamma2- and PKD-mediated transport to the cell surface and the organization of the Golgi apparatus.The Journal of cell biology · 2005Article
- Structural requirements for localization and activation of protein kinase C mu (PKC mu) at the Golgi compartment.The Journal of cell biology · 2002Article
- Protein kinase Cepsilon actin-binding site is important for neurite outgrowth during neuronal differentiation.Molecular biology of the cell · 2002Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein kinase C (PKC) is a multigene family of serine/threonine kinases that are central to many signal transduction pathways. Among the PKC isozymes, only PKC epsilon has been reported to exhibit full oncogenic potential. PKC epsilon also displays unique substrate specificity and intracellular localization. To examine the interrelationship between the biological effects and domain structure of PKC epsilon, NIH 3T3 cells were stably transfected to overexpress different epitope-tagged fragments of PKC epsilon. The overexpressed proteins each contain the epsilon-tag peptide at the C terminus to allow ready detection with an antibody specific for the tag. The holo-PKC epsilon was found to localize with the Golgi network and other compartments, whereas the zinc-finger domain localized exclusively at the Golgi. Golgi-specific glycosaminoglycan sulfation was strongly inhibited in cells overexpressing either holo-PKC epsilon or its zinc-finger domain, while the secretion of sulfated glycosaminoglycans into the medium was impaired in cells expressing the PKC epsilon zinc-finger domain. Thus, these results suggest that PKC epsilon may be involved in specifically regulating Golgi-related processes. Further, the results indicate that PKC epsilon domains other than the kinase domain may also have biological activity and that the zinc-finger domain may function as a subcellular localization signal.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.