Peripherin-2 differentially interacts with cone opsins in outer segments of cone photoreceptors

Publikationstyp:
Zeitschriftenaufsatz
Metadaten:
Autoren
  • ON Phuong Nguyen
  • Sybille Boehm
  • Andreas Giel
  • Elisabeth S Butz
  • Uwe Wolfrum
  • Johann H Brandstaetter
  • Christian Wahl-Schott
  • Martin Biel
  • Elvir Becirovic
Autoren-URL
https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000393062900001&DestLinkType=FullRecord&DestApp=WOS_CPL
DOI
10.1093/hmg/ddw103
eISSN
1460-2083
Externe Identifier
  • Clarivate Analytics Document Solution ID: EJ2TA
  • PubMed Identifier: 27033727
ISSN
0964-6906
Ausgabe der Veröffentlichung
12
Zeitschrift
HUMAN MOLECULAR GENETICS
Paginierung
2367 - 2377
Datum der Veröffentlichung
2016
Status
Published
Titel
Peripherin-2 differentially interacts with cone opsins in outer segments of cone photoreceptors
Sub types
  • Article
Ausgabe der Zeitschrift
25

Datenquelle: Web of Science (Lite)

Andere Metadatenquellen:
Autoren
  • ON Phuong Nguyen
  • Sybille Böhm
  • Andreas Gießl
  • Elisabeth S Butz
  • Uwe Wolfrum
  • Johann H Brandstätter
  • Christian Wahl-Schott
  • Martin Biel
  • Elvir Becirovic
DOI
10.1093/hmg/ddw103
eISSN
1460-2083
ISSN
0964-6906
Zeitschrift
Human Molecular Genetics
Sprache
en
Online publication date
2016
Paginierung
ddw103 - ddw103
Status
Published online
Herausgeber
Oxford University Press (OUP)
Herausgeber URL
http://dx.doi.org/10.1093/hmg/ddw103
Datum der Datenerfassung
2017
Titel
Peripherin-2 differentially interacts with cone opsins in outer segments of cone photoreceptors

Datenquelle: Crossref

Abstract
Peripherin-2 is a glycomembrane protein exclusively expressed in the light-sensing compartments of rod and cone photoreceptors designated as outer segments (OS). Mutations in peripherin-2 are associated with degenerative retinal diseases either affecting rod or cone photoreceptors. While peripherin-2 has been extensively studied in rods, there is only little information on its supramolecular organization and function in cones. Recently, we have demonstrated that peripherin-2 interacts with the light detector rhodopsin in OS of rods. It remains unclear, however, if peripherin-2 also binds to cone opsins. Here, using a combination of co-immunoprecipitation analyses, transmission electron microscopy (TEM)-based immunolabeling experiments, and quantitative fluorescence resonance energy transfer (FRET) measurements in cone OS of wild type mice, we demonstrate that peripherin-2 binds to both, S-opsin and M-opsin. However, FRET-based quantification of the respective interactions indicated significantly less stringent binding of peripherin-2 to S-opsin compared to its interaction with M-opsin. Subsequent TEM-studies also showed less co-localization of peripherin-2 and S-opsin in cone OS compared to peripherin-2 and M-opsin. Furthermore, quantitative FRET analysis in acutely isolated cone OS revealed that the cone degeneration-causing V268I mutation in peripherin-2 selectively reduced binding to M-opsin without affecting the peripherin-2 interaction to S-opsin or rhodopsin. The differential binding of peripherin-2 to cone opsins and the mutant-specific interference with the peripherin-2/M-opsin binding points to a novel role of peripherin-2 in cones and might contribute to understanding the differential penetrance of certain peripherin-2 mutations in rods and cones. Finally, our results provide a proof-of-principle for quantitative FRET measurements of protein-protein interactions in cone OS.
Addresses
  • Munich Center for Integrated Protein Science CIPS , 81377 München, Germany, elvir.becirovic@cup.uni-muenchen.de martin.biel@cup.uni-muenchen.de.
Autoren
  • ON Phuong Nguyen
  • Sybille Böhm
  • Andreas Gießl
  • Elisabeth S Butz
  • Uwe Wolfrum
  • Johann H Brandstätter
  • Christian Wahl-Schott
  • Martin Biel
  • Elvir Becirovic
DOI
10.1093/hmg/ddw103
eISSN
1460-2083
Externe Identifier
  • PubMed Identifier: 27033727
Open access
false
ISSN
0964-6906
Ausgabe der Veröffentlichung
12
Zeitschrift
Human molecular genetics
Schlüsselwörter
  • Retina
  • Animals
  • Humans
  • Mice
  • Retinal Degeneration
  • Rhodopsin
  • Antigens, Neoplasm
  • Microscopy, Electron, Transmission
  • Fluorescence Resonance Energy Transfer
  • Protein Binding
  • Mutation
  • Retinal Cone Photoreceptor Cells
  • Cone Opsins
Sprache
eng
Medium
Print-Electronic
Online publication date
2016
Paginierung
2367 - 2377
Datum der Veröffentlichung
2016
Status
Published
Datum der Datenerfassung
2016
Titel
Peripherin-2 differentially interacts with cone opsins in outer segments of cone photoreceptors.
Sub types
  • Research Support, Non-U.S. Gov't
  • Journal Article
Ausgabe der Zeitschrift
25

Datenquelle: Europe PubMed Central

Abstract
Peripherin-2 is a glycomembrane protein exclusively expressed in the light-sensing compartments of rod and cone photoreceptors designated as outer segments (OS). Mutations in peripherin-2 are associated with degenerative retinal diseases either affecting rod or cone photoreceptors. While peripherin-2 has been extensively studied in rods, there is only little information on its supramolecular organization and function in cones. Recently, we have demonstrated that peripherin-2 interacts with the light detector rhodopsin in OS of rods. It remains unclear, however, if peripherin-2 also binds to cone opsins. Here, using a combination of co-immunoprecipitation analyses, transmission electron microscopy (TEM)-based immunolabeling experiments, and quantitative fluorescence resonance energy transfer (FRET) measurements in cone OS of wild type mice, we demonstrate that peripherin-2 binds to both, S-opsin and M-opsin. However, FRET-based quantification of the respective interactions indicated significantly less stringent binding of peripherin-2 to S-opsin compared to its interaction with M-opsin. Subsequent TEM-studies also showed less co-localization of peripherin-2 and S-opsin in cone OS compared to peripherin-2 and M-opsin. Furthermore, quantitative FRET analysis in acutely isolated cone OS revealed that the cone degeneration-causing V268I mutation in peripherin-2 selectively reduced binding to M-opsin without affecting the peripherin-2 interaction to S-opsin or rhodopsin. The differential binding of peripherin-2 to cone opsins and the mutant-specific interference with the peripherin-2/M-opsin binding points to a novel role of peripherin-2 in cones and might contribute to understanding the differential penetrance of certain peripherin-2 mutations in rods and cones. Finally, our results provide a proof-of-principle for quantitative FRET measurements of protein-protein interactions in cone OS.
Date of acceptance
2016
Autoren
  • ON Phuong Nguyen
  • Sybille Böhm
  • Andreas Gießl
  • Elisabeth S Butz
  • Uwe Wolfrum
  • Johann H Brandstätter
  • Christian Wahl-Schott
  • Martin Biel
  • Elvir Becirovic
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/27033727
DOI
10.1093/hmg/ddw103
eISSN
1460-2083
Ausgabe der Veröffentlichung
12
Zeitschrift
Hum Mol Genet
Schlüsselwörter
  • Animals
  • Antigens, Neoplasm
  • Cone Opsins
  • Fluorescence Resonance Energy Transfer
  • Humans
  • Mice
  • Microscopy, Electron, Transmission
  • Mutation
  • Protein Binding
  • Retina
  • Retinal Cone Photoreceptor Cells
  • Retinal Degeneration
  • Rhodopsin
Sprache
eng
Country
England
Paginierung
2367 - 2377
PII
ddw103
Datum der Veröffentlichung
2016
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2017
Titel
Peripherin-2 differentially interacts with cone opsins in outer segments of cone photoreceptors.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
25

Datenquelle: PubMed

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