For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
0
views
173
references
 Top references
cited by
9
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      535
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      PKC regulation of ion channels: The involvement of PIP 2

      review-article
      Author(s): 1 , 1 , 2 , 3 , ∗
      Publication date (Electronic):
      Journal: The Journal of Biological Chemistry
      Publisher: American Society for Biochemistry and Molecular Biology
      Keywords: PKC, phosphatidylinositol (4,5) bisphosphate, ion channel, phosphorylation, voltage-gated potassium channel, inwardly rectifying potassium channels, transient receptor potential channels, ASIC, acid-sensing ion channel, BIM, bisindolylmaleimide, CaCC, Ca2+-activated chloride channel, CaV, voltage-gated calcium, ClC, chloride channel, CFTR, cystic fibrosis transmembrane conductance regulator, cPKC, conventional PKC, DAG, diacylglycerol, diC8-PIP2, dioctanoyl PI(4,5)P2, DRG, dorsal root ganglia, ENaC, epithelial Na+ channel, GIRK, G-protein-gated inwardly rectifying K+ channel, K2P, two-pore domain potassium, KCa, calcium-activated potassium, Kir, inwardly rectifying potassium, KV, voltage-gated potassium, LQTS, long QT syndrome, MD, molecular dynamics, MOR, μ-opioid receptor, MS, mass spectrometry, nPKC, novel PKC, PdBu, phorbol 12,13-dibutyrate, PI(4,5)P2 or PIP2, phosphatidylinositol (4,5) bisphosphate, PMA, phorbol 12-myristate 13-acetate, SUR, sulfonylurea receptor subunit, TMTX, thymeleatoxin, TRP, transient receptor potential, TRPC, TRP canonical, TRPM, TRP melastatin, TRPP, TRP polycystic, TRPV, TRP vanilloid, TTX, tetrodotoxin, VSD, voltage sensor domain

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Ion channels are integral membrane proteins whose gating has been increasingly shown to depend on the presence of the low-abundance membrane phospholipid, phosphatidylinositol (4,5) bisphosphate. The expression and function of ion channels is tightly regulated via protein phosphorylation by specific kinases, including various PKC isoforms. Several channels have further been shown to be regulated by PKC through altered surface expression, probability of channel opening, shifts in voltage dependence of their activation, or changes in inactivation or desensitization. In this review, we survey the impact of phosphorylation of various ion channels by PKC isoforms and examine the dependence of phosphorylated ion channels on phosphatidylinositol (4,5) bisphosphate as a mechanistic endpoint to control channel gating.

          Related collections

          Most cited references173

          • Record: found
          • Abstract: found
          • Article: found
          Is Open Access

          PhosphoSitePlus, 2014: mutations, PTMs and recalibrations

          Peter V. Hornbeck, Bin Zhang, Beth Murray … (2014)
          PhosphoSitePlus® (PSP, http://www.phosphosite.org/), a knowledgebase dedicated to mammalian post-translational modifications (PTMs), contains over 330 000 non-redundant PTMs, including phospho, acetyl, ubiquityl and methyl groups. Over 95% of the sites are from mass spectrometry (MS) experiments. In order to improve data reliability, early MS data have been reanalyzed, applying a common standard of analysis across over 1 000 000 spectra. Site assignments with P > 0.05 were filtered out. Two new downloads are available from PSP. The ‘Regulatory sites’ dataset includes curated information about modification sites that regulate downstream cellular processes, molecular functions and protein-protein interactions. The ‘PTMVar’ dataset, an intersect of missense mutations and PTMs from PSP, identifies over 25 000 PTMVars (PTMs Impacted by Variants) that can rewire signaling pathways. The PTMVar data include missense mutations from UniPROTKB, TCGA and other sources that cause over 2000 diseases or syndromes (MIM) and polymorphisms, or are associated with hundreds of cancers. PTMVars include 18 548 phosphorlyation sites, 3412 ubiquitylation sites, 2316 acetylation sites, 685 methylation sites and 245 succinylation sites.
          Article 0 comments Cited 733 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: found
            Is Open Access

            THE CONCISE GUIDE TO PHARMACOLOGY 2019/20: Introduction and Other Protein Targets

            Stephen Ph Alexander, Eamonn Kelly, Alistair Mathie … (2019)
            The Concise Guide to PHARMACOLOGY 2019/20 is the fourth in this series of biennial publications. The Concise Guide provides concise overviews of the key properties of nearly 1800 human drug targets with an emphasis on selective pharmacology (where available), plus links to the open access knowledgebase source of drug targets and their ligands (http://www.guidetopharmacology.org/), which provides more detailed views of target and ligand properties. Although the Concise Guide represents approximately 400 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point‐in‐time record that will survive database updates. The full contents of this section can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.14747. In addition to this overview, in which are identified Other protein targets which fall outside of the subsequent categorisation, there are six areas of focus: G protein‐coupled receptors, ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The landscape format of the Concise Guide is designed to facilitate comparison of related targets from material contemporary to mid‐2019, and supersedes data presented in the 2017/18, 2015/16 and 2013/14 Concise Guides and previous Guides to Receptors and Channels. It is produced in close conjunction with the International Union of Basic and Clinical Pharmacology Committee on Receptor Nomenclature and Drug Classification (NC‐IUPHAR), therefore, providing official IUPHAR classification and nomenclature for human drug targets, where appropriate.
            Article 0 comments Cited 173 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Protein kinase C and lipid signaling for sustained cellular responses.

              Y Nishizuka (1995)
              Since the second messenger role was proposed for the products of inositol phospholipid hydrolysis, considerable progress has been made in our understanding of the biochemical mechanism of the intracellular signaling network. It is now becoming evident that stimulation of a cell surface receptor initiates a degradation cascade of various membrane lipid constituents. Many of their metabolites have potential to induce, intensify, and prolong the activation of protein kinase C that is needed for sustained cellular responses.
              Article 0 comments Cited 171 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Contributors
                Diomedes E. Logothetis
                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: 16 May 2022
                Publication date Collection: June 2022
                Publication date (Electronic): 16 May 2022
                Volume: 298
                Issue: 6
                Electronic Location Identifier: 102035
                Affiliations
                [1 ]Department of Pharmaceutical Sciences, Bouvé College of Health Sciences and College of Science, Northeastern University, Boston, Massachusetts, USA
                [2 ]Department of Chemistry and Chemical Biology, Bouvé College of Health Sciences and College of Science, Northeastern University, Boston, Massachusetts, USA
                [3 ]Center for Drug Discovery, Bouvé College of Health Sciences and College of Science, Northeastern University, Boston, Massachusetts, USA
                Author notes
                [∗ ]For correspondence: Diomedes E. Logothetis d.logothetis@ 123456northeastern.edu
                Article
                Publisher Item ID: S0021-9258(22)00475-6 Publisher ID: 102035
                DOI: 10.1016/j.jbc.2022.102035
                PMC ID: 9198471
                PubMed ID: 35588786
                SO-VID: 5df7ef2d-0a1f-4118-a508-3bb6eccbdacc
                Copyright © © 2022 The Authors
                License:

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

                History
                Date received : 17 February 2022
                Date revision received : 10 May 2022
                Categories
                Subject: JBC Reviews

                ScienceOpen disciplines: Biochemistry
                Keywords: pkc,phosphatidylinositol (4,5) bisphosphate,ion channel, phosphorylation,voltage-gated potassium channel,inwardly rectifying potassium channels,transient receptor potential channels,asic, acid-sensing ion channel,bim, bisindolylmaleimide,cacc, ca2+-activated chloride channel,cav, voltage-gated calcium,clc, chloride channel,cftr, cystic fibrosis transmembrane conductance regulator,cpkc, conventional pkc,dag, diacylglycerol,dic8-pip2, dioctanoyl pi(4,5)p2,drg, dorsal root ganglia,enac, epithelial na+ channel,girk, g-protein-gated inwardly rectifying k+ channel,k2p, two-pore domain potassium,kca, calcium-activated potassium,kir, inwardly rectifying potassium,kv, voltage-gated potassium,lqts, long qt syndrome,md, molecular dynamics,mor, μ-opioid receptor,ms, mass spectrometry,npkc, novel pkc,pdbu, phorbol 12,13-dibutyrate,pi(4,5)p2 or pip2, phosphatidylinositol (4,5) bisphosphate,pma, phorbol 12-myristate 13-acetate,sur, sulfonylurea receptor subunit,tmtx, thymeleatoxin,trp, transient receptor potential,trpc, trp canonical,trpm, trp melastatin,trpp, trp polycystic,trpv, trp vanilloid,ttx, tetrodotoxin,vsd, voltage sensor domain
                Data availability:
                ScienceOpen disciplines: Biochemistry
                Keywords: pkc, phosphatidylinositol (4,5) bisphosphate, ion channel, phosphorylation, voltage-gated potassium channel, inwardly rectifying potassium channels, transient receptor potential channels, asic, acid-sensing ion channel, bim, bisindolylmaleimide, cacc, ca2+-activated chloride channel, cav, voltage-gated calcium, clc, chloride channel, cftr, cystic fibrosis transmembrane conductance regulator, cpkc, conventional pkc, dag, diacylglycerol, dic8-pip2, dioctanoyl pi(4,5)p2, drg, dorsal root ganglia, enac, epithelial na+ channel, girk, g-protein-gated inwardly rectifying k+ channel, k2p, two-pore domain potassium, kca, calcium-activated potassium, kir, inwardly rectifying potassium, kv, voltage-gated potassium, lqts, long qt syndrome, md, molecular dynamics, mor, μ-opioid receptor, ms, mass spectrometry, npkc, novel pkc, pdbu, phorbol 12,13-dibutyrate, pi(4,5)p2 or pip2, phosphatidylinositol (4,5) bisphosphate, pma, phorbol 12-myristate 13-acetate, sur, sulfonylurea receptor subunit, tmtx, thymeleatoxin, trp, transient receptor potential, trpc, trp canonical, trpm, trp melastatin, trpp, trp polycystic, trpv, trp vanilloid, ttx, tetrodotoxin, vsd, voltage sensor domain

                Comments

                Comment on this article

                scite_

                Similar content535

                See all similar

                Cited by9

                See all cited by

                Most referenced authors2,564

                See all reference authors