Interaction of glutamic-acid-rich proteins with the cGMP signalling pathway in rod photoreceptors
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Uwe Wolfrum
- Sammlungen
- metadata
- ISSN
- 0028-0836
- Ausgabe der Veröffentlichung
- 6746
- Zeitschrift
- Nature
- Schlüsselwörter
- 500 Naturwissenschaften
- 500 Natural sciences and mathematics
- Sprache
- eng
- Paginierung
- Seiten: 761 - 766
- Datum der Veröffentlichung
- 1999
- Herausgeber
- Nature Publ. Group
- Datum der Datenerfassung
- 2020
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2020
- Zugang
- Public
- Titel
- Interaction of glutamic-acid-rich proteins with the cGMP signalling pathway in rod photoreceptors
- Ausgabe der Zeitschrift
- 400
Datenquelle: METADATA.UB
- Andere Metadatenquellen:
-
- Autoren
- HG Körschen
- M Beyermann
- F Müller
- M Heck
- M Vantler
- KW Koch
- R Kellner
- U Wolfrum
- C Bode
- KP Hofmann
- UB Kaupp
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000082131100049&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1038/23468
- eISSN
- 1476-4687
- Externe Identifier
- Clarivate Analytics Document Solution ID: 228HM
- PubMed Identifier: 10466724
- ISSN
- 0028-0836
- Ausgabe der Veröffentlichung
- 6746
- Zeitschrift
- NATURE
- Paginierung
- 761 - 766
- Datum der Veröffentlichung
- 1999
- Status
- Published
- Titel
- Interaction of glutamic-acid-rich proteins with the cGMP signalling pathway in rod photoreceptors
- Sub types
- Article
- Ausgabe der Zeitschrift
- 400
Datenquelle: Web of Science (Lite)
- Autoren
- Heinz G Körschen
- Michael Beyermann
- Frank Müller
- Martin Heck
- Marius Vantler
- Karl-Wilhelm Koch
- Roland Kellner
- Uwe Wolfrum
- Christian Bode
- Klaus Peter Hofmann
- U Benjamin Kaupp
- DOI
- 10.1038/23468
- eISSN
- 1476-4687
- ISSN
- 0028-0836
- Ausgabe der Veröffentlichung
- 6746
- Zeitschrift
- Nature
- Sprache
- en
- Paginierung
- 761 - 766
- Datum der Veröffentlichung
- 1999
- Status
- Published
- Herausgeber
- Springer Science and Business Media LLC
- Herausgeber URL
- http://dx.doi.org/10.1038/23468
- Datum der Datenerfassung
- 2021
- Titel
- Interaction of glutamic-acid-rich proteins with the cGMP signalling pathway in rod photoreceptors
- Ausgabe der Zeitschrift
- 400
Datenquelle: Crossref
- Abstract
- The assembly of signalling molecules into macromolecular complexes (transducisomes) provides specificity, sensitivity and speed in intracellular signalling pathways. Rod photoreceptors in the eye contain an unusual set of glutamic-acid-rich proteins (GARPs) of unknown function. GARPs exist as two soluble forms, GARP1 and GARP2, and as a large cytoplasmic domain (GARP' part) of the beta-subunit of the cyclic GMP-gated channel. Here we identify GARPs as multivalent proteins that interact with the key players of cGMP signalling, phosphodiesterase and guanylate cyclase, and with a retina-specific ATP-binding cassette transporter (ABCR), through four, short, repetitive sequences. In electron micrographs, GARPs are restricted to the rim region and incisures of discs in close proximity to the guanylate cyclase and ABCR, whereas the phosphodiesterase is randomly distributed. GARP2, the most abundant splice form, associates more strongly with light-activated than with inactive phosphodiesterase, and GARP2 potently inhibits phosphodiesterase activity. Thus, the GARPs organize a dynamic protein complex near the disc rim that may control cGMP turnover and possibly other light-dependent processes. Because there are no similar GARPs in cones, we propose that GARPs may prevent unnecessary cGMP turnover during daylight, when rods are held in saturation by the relatively high light levels.
- Addresses
- Institut für Biologische Informationsverarbeitung, Forschungszentrum Jülich, Germany.
- Autoren
- HG Körschen
- M Beyermann
- F Müller
- M Heck
- M Vantler
- KW Koch
- R Kellner
- U Wolfrum
- C Bode
- KP Hofmann
- UB Kaupp
- DOI
- 10.1038/23468
- eISSN
- 1476-4687
- Externe Identifier
- PubMed Identifier: 10466724
- Open access
- false
- ISSN
- 0028-0836
- Ausgabe der Veröffentlichung
- 6746
- Zeitschrift
- Nature
- Schlüsselwörter
- Animals
- Cattle
- Transducin
- Phosphoric Diester Hydrolases
- Guanylate Cyclase
- Glutamic Acid
- Proteins
- ATP-Binding Cassette Transporters
- Eye Proteins
- Nerve Tissue Proteins
- Recombinant Proteins
- Cyclic GMP
- Phosphodiesterase Inhibitors
- Signal Transduction
- Amino Acid Sequence
- Protein Binding
- Molecular Sequence Data
- Cyclic Nucleotide-Gated Cation Channels
- Rod Cell Outer Segment
- Retinal Rod Photoreceptor Cells
- In Vitro Techniques
- Sprache
- eng
- Medium
- Paginierung
- 761 - 766
- Datum der Veröffentlichung
- 1999
- Status
- Published
- Datum der Datenerfassung
- 1999
- Titel
- Interaction of glutamic-acid-rich proteins with the cGMP signalling pathway in rod photoreceptors.
- Sub types
- Research Support, Non-U.S. Gov't
- Journal Article
- Ausgabe der Zeitschrift
- 400
Datenquelle: Europe PubMed Central
- Abstract
- The assembly of signalling molecules into macromolecular complexes (transducisomes) provides specificity, sensitivity and speed in intracellular signalling pathways. Rod photoreceptors in the eye contain an unusual set of glutamic-acid-rich proteins (GARPs) of unknown function. GARPs exist as two soluble forms, GARP1 and GARP2, and as a large cytoplasmic domain (GARP' part) of the beta-subunit of the cyclic GMP-gated channel. Here we identify GARPs as multivalent proteins that interact with the key players of cGMP signalling, phosphodiesterase and guanylate cyclase, and with a retina-specific ATP-binding cassette transporter (ABCR), through four, short, repetitive sequences. In electron micrographs, GARPs are restricted to the rim region and incisures of discs in close proximity to the guanylate cyclase and ABCR, whereas the phosphodiesterase is randomly distributed. GARP2, the most abundant splice form, associates more strongly with light-activated than with inactive phosphodiesterase, and GARP2 potently inhibits phosphodiesterase activity. Thus, the GARPs organize a dynamic protein complex near the disc rim that may control cGMP turnover and possibly other light-dependent processes. Because there are no similar GARPs in cones, we propose that GARPs may prevent unnecessary cGMP turnover during daylight, when rods are held in saturation by the relatively high light levels.
- Autoren
- HG Körschen
- M Beyermann
- F Müller
- M Heck
- M Vantler
- KW Koch
- R Kellner
- U Wolfrum
- C Bode
- KP Hofmann
- UB Kaupp
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/10466724
- DOI
- 10.1038/23468
- ISSN
- 0028-0836
- Ausgabe der Veröffentlichung
- 6746
- Zeitschrift
- Nature
- Schlüsselwörter
- ATP-Binding Cassette Transporters
- Amino Acid Sequence
- Animals
- Cattle
- Cyclic GMP
- Cyclic Nucleotide-Gated Cation Channels
- Eye Proteins
- Glutamic Acid
- Guanylate Cyclase
- In Vitro Techniques
- Molecular Sequence Data
- Nerve Tissue Proteins
- Phosphodiesterase Inhibitors
- Phosphoric Diester Hydrolases
- Protein Binding
- Proteins
- Recombinant Proteins
- Retinal Rod Photoreceptor Cells
- Rod Cell Outer Segment
- Signal Transduction
- Transducin
- Sprache
- eng
- Country
- England
- Paginierung
- 761 - 766
- Datum der Veröffentlichung
- 1999
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 1999
- Titel
- Interaction of glutamic-acid-rich proteins with the cGMP signalling pathway in rod photoreceptors.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 400
Datenquelle: PubMed
- Beziehungen:
- Eigentum von