A novel Usher protein network at the periciliary reloading point between molecular transport machineries in vertebrate photoreceptor cells

Publication type:
Journal article
Metadata:
Autoren
  • Tina Maerker
  • Erwin van Wijk
  • Nora Overlack
  • Ferry FJ Kersten
  • JoAnn McGee
  • Tobias Goldmann
  • Elisabeth Sehn
  • Ronald Roepman
  • Edward J Walsh
  • Hannie Kremer
  • Uwe Wolfrum
Autoren-URL
https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000251866600006&DestLinkType=FullRecord&DestApp=WOS_CPL
DOI
10.1093/hmg/ddm285
eISSN
1460-2083
Externe Identifier
  • Clarivate Analytics Document Solution ID: 244LE
  • PubMed Identifier: 17906286
ISSN
0964-6906
Ausgabe der Veröffentlichung
1
Zeitschrift
HUMAN MOLECULAR GENETICS
Paginierung
71 - 86
Datum der Veröffentlichung
2008
Status
Published
Titel
A novel Usher protein network at the periciliary reloading point between molecular transport machineries in vertebrate photoreceptor cells
Sub types
  • Article
Ausgabe der Zeitschrift
17

Data source: Web of Science (Lite)

Other metadata sources:
Autoren
  • Tina Maerker
  • Erwin van Wijk
  • Nora Overlack
  • Ferry FJ Kersten
  • JoAnn McGee
  • Tobias Goldmann
  • Elisabeth Sehn
  • Ronald Roepman
  • Edward J Walsh
  • Hannie Kremer
  • Uwe Wolfrum
DOI
10.1093/hmg/ddm285
eISSN
1460-2083
ISSN
0964-6906
Ausgabe der Veröffentlichung
1
Zeitschrift
Human Molecular Genetics
Sprache
en
Online publication date
2007
Paginierung
71 - 86
Datum der Veröffentlichung
2008
Status
Published
Herausgeber
Oxford University Press (OUP)
Herausgeber URL
http://dx.doi.org/10.1093/hmg/ddm285
Datum der Datenerfassung
2021
Titel
A novel Usher protein network at the periciliary reloading point between molecular transport machineries in vertebrate photoreceptor cells
Ausgabe der Zeitschrift
17

Data source: Crossref

Abstract
The human Usher syndrome (USH) is the most frequent cause of combined deaf-blindness. USH is genetically heterogeneous with at least 12 chromosomal loci assigned to three clinical types, USH1-3. Although these USH types exhibit similar phenotypes in human, the corresponding gene products belong to very different protein classes and families. The scaffold protein harmonin (USH1C) was shown to integrate all identified USH1 and USH2 molecules into protein networks. Here, we analyzed a protein network organized in the absence of harmonin by the scaffold proteins SANS (USH1G) and whirlin (USH2D). Immunoelectron microscopic analyses disclosed the colocalization of all network components in the apical inner segment collar and the ciliary apparatus of mammalian photoreceptor cells. In this complex, whirlin and SANS directly interact. Furthermore, SANS provides a linkage to the microtubule transport machinery, whereas whirlin may anchor USH2A isoform b and VLGR1b (very large G-protein coupled receptor 1b) via binding to their cytodomains at specific membrane domains. The long ectodomains of both transmembrane proteins extend into the gap between the adjacent membranes of the connecting cilium and the apical inner segment. Analyses of Vlgr1/del7TM mice revealed the ectodomain of VLGR1b as a component of fibrous links present in this gap. Comparative analyses of mouse and Xenopus photoreceptors demonstrated that this USH protein network is also part of the periciliary ridge complex in Xenopus. Since this structural specialization in amphibian photoreceptor cells defines a specialized membrane domain for docking and fusion of transport vesicles, we suggest a prominent role of the USH proteins in cargo shipment.
Addresses
  • Department of Cell and Matrix Biology, Institute of Zoology, Johannes Gutenberg University of Mainz, 55099 Mainz, Germany.
Autoren
  • Tina Maerker
  • Erwin van Wijk
  • Nora Overlack
  • Ferry FJ Kersten
  • Joann McGee
  • Tobias Goldmann
  • Elisabeth Sehn
  • Ronald Roepman
  • Edward J Walsh
  • Hannie Kremer
  • Uwe Wolfrum
DOI
10.1093/hmg/ddm285
eISSN
1460-2083
Externe Identifier
  • PubMed Identifier: 17906286
Funding acknowledgements
  • NEI NIH HHS: EY016247
Open access
false
ISSN
0964-6906
Ausgabe der Veröffentlichung
1
Zeitschrift
Human molecular genetics
Schlüsselwörter
  • COS Cells
  • NIH 3T3 Cells
  • Subcellular Fractions
  • Animals
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Xenopus
  • Humans
  • Mice
  • Adaptor Proteins, Signal Transducing
  • Cell Cycle Proteins
  • Cytoskeletal Proteins
  • Membrane Proteins
  • Receptors, G-Protein-Coupled
  • Nerve Tissue Proteins
  • Extracellular Matrix Proteins
  • Microscopy, Immunoelectron
  • Transfection
  • Protein Interaction Mapping
  • Models, Biological
  • Usher Syndromes
  • Photoreceptor Cells, Vertebrate
  • In Vitro Techniques
  • Chlorocebus aethiops
Sprache
eng
Medium
Print-Electronic
Online publication date
2007
Paginierung
71 - 86
Datum der Veröffentlichung
2008
Status
Published
Datum der Datenerfassung
2007
Titel
A novel Usher protein network at the periciliary reloading point between molecular transport machineries in vertebrate photoreceptor cells.
Sub types
  • Research Support, Non-U.S. Gov't
  • Journal Article
  • Research Support, N.I.H., Extramural
Ausgabe der Zeitschrift
17

Data source: Europe PubMed Central

Abstract
The human Usher syndrome (USH) is the most frequent cause of combined deaf-blindness. USH is genetically heterogeneous with at least 12 chromosomal loci assigned to three clinical types, USH1-3. Although these USH types exhibit similar phenotypes in human, the corresponding gene products belong to very different protein classes and families. The scaffold protein harmonin (USH1C) was shown to integrate all identified USH1 and USH2 molecules into protein networks. Here, we analyzed a protein network organized in the absence of harmonin by the scaffold proteins SANS (USH1G) and whirlin (USH2D). Immunoelectron microscopic analyses disclosed the colocalization of all network components in the apical inner segment collar and the ciliary apparatus of mammalian photoreceptor cells. In this complex, whirlin and SANS directly interact. Furthermore, SANS provides a linkage to the microtubule transport machinery, whereas whirlin may anchor USH2A isoform b and VLGR1b (very large G-protein coupled receptor 1b) via binding to their cytodomains at specific membrane domains. The long ectodomains of both transmembrane proteins extend into the gap between the adjacent membranes of the connecting cilium and the apical inner segment. Analyses of Vlgr1/del7TM mice revealed the ectodomain of VLGR1b as a component of fibrous links present in this gap. Comparative analyses of mouse and Xenopus photoreceptors demonstrated that this USH protein network is also part of the periciliary ridge complex in Xenopus. Since this structural specialization in amphibian photoreceptor cells defines a specialized membrane domain for docking and fusion of transport vesicles, we suggest a prominent role of the USH proteins in cargo shipment.
Autoren
  • Tina Maerker
  • Erwin van Wijk
  • Nora Overlack
  • Ferry FJ Kersten
  • Joann McGee
  • Tobias Goldmann
  • Elisabeth Sehn
  • Ronald Roepman
  • Edward J Walsh
  • Hannie Kremer
  • Uwe Wolfrum
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/17906286
DOI
10.1093/hmg/ddm285
Funding acknowledgements
  • NEI NIH HHS: EY016247
ISSN
0964-6906
Ausgabe der Veröffentlichung
1
Zeitschrift
Hum Mol Genet
Schlüsselwörter
  • Adaptor Proteins, Signal Transducing
  • Animals
  • COS Cells
  • Cell Cycle Proteins
  • Chlorocebus aethiops
  • Cytoskeletal Proteins
  • Extracellular Matrix Proteins
  • Humans
  • In Vitro Techniques
  • Membrane Proteins
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Microscopy, Immunoelectron
  • Models, Biological
  • NIH 3T3 Cells
  • Nerve Tissue Proteins
  • Photoreceptor Cells, Vertebrate
  • Protein Interaction Mapping
  • Receptors, G-Protein-Coupled
  • Subcellular Fractions
  • Transfection
  • Usher Syndromes
  • Xenopus
Sprache
eng
Country
England
Paginierung
71 - 86
PII
ddm285
Datum der Veröffentlichung
2008
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2008
Titel
A novel Usher protein network at the periciliary reloading point between molecular transport machineries in vertebrate photoreceptor cells.
Sub types
  • Journal Article
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
17

Data source: PubMed

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