R9AP targeting to rod outer segments is independent of rhodopsin and is guided by the SNARE homology domain

Jillian N Pearring; Eric C Lieu; Joan R Winter; Sheila A Baker; Vadim Y Arshavsky

doi:10.1091/mbc.E14-02-0747

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R9AP targeting to rod outer segments is independent of rhodopsin and is guided by the SNARE homology domain

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R9AP targeting to rod outer segments is independent of rhodopsin and is guided by the SNARE homology domain

Jillian N Pearring, Eric C Lieu, Joan R Winter, Sheila A Baker and Vadim Y Arshavsky

Molecular biology of the cell, Vol.25(17), pp.2644-2649

09/01/2014

DOI: 10.1091/mbc.E14-02-0747

PMCID: PMC4148253

PMID: 25009288

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Abstract

In vertebrate photoreceptor cells, rapid recovery from light excitation is dependent on the RGS9⋅Gβ5 GTPase-activating complex located in the light-sensitive outer segment organelle. RGS9⋅Gβ5 is tethered to the outer segment membranes by its membrane anchor, R9AP. Recent studies indicated that RGS9⋅Gβ5 possesses targeting information that excludes it from the outer segment and that this information is overridden by association with R9AP, which allows outer segment targeting of the entire complex. It was also proposed that R9AP itself does not contain specific targeting information and instead is delivered to the outer segment in the same post-Golgi vesicles as rhodopsin, because they are the most abundant transport vesicles in photoreceptor cells. In this study, we revisited this concept by analyzing R9AP targeting in rods of wild-type and rhodopsin-knockout mice. We found that the R9AP targeting mechanism does not require the presence of rhodopsin and further demonstrated that R9AP is actively targeted in rods by its SNARE homology domain.

Protein Structure, Tertiary

Animals

Rhodopsin - genetics

Membrane Proteins - chemistry

Rod Cell Outer Segment - metabolism

Mice, Inbred C57BL

Membrane Proteins - metabolism

Mice

Amino Acid Motifs

Mice, Knockout

Protein Transport

Details

Title: Subtitle: R9AP targeting to rod outer segments is independent of rhodopsin and is guided by the SNARE homology domain
Creators: Jillian N Pearring - Albert Eye Research Institute, Duke Eye Center, Duke University, Durham, NC 27710
Eric C Lieu - Albert Eye Research Institute, Duke Eye Center, Duke University, Durham, NC 27710
Joan R Winter - Albert Eye Research Institute, Duke Eye Center, Duke University, Durham, NC 27710
Sheila A Baker - Department of Biochemistry and Ophthalmology and Visual Sciences, Carver College of Medicine, University of Iowa, Iowa City, IA 52242
Vadim Y Arshavsky - Albert Eye Research Institute, Duke Eye Center, Duke University, Durham, NC 27710 vadim.arshavsky@duke.edu
Resource Type: Journal article
Publication Details: Molecular biology of the cell, Vol.25(17), pp.2644-2649
DOI: 10.1091/mbc.E14-02-0747
PMID: 25009288
PMCID: PMC4148253
NLM abbreviation: Mol Biol Cell
ISSN: 1059-1524
eISSN: 1939-4586
Publisher: American Society for Cell Biology; United States
Grant note: R01 EY020542 / NEI NIH HHS EY12859 / NEI NIH HHS EY22508 / NEI NIH HHS EY5722 / NEI NIH HHS R01 EY012859 / NEI NIH HHS P30 EY005722 / NEI NIH HHS F32 EY022508 / NEI NIH HHS EY20542 / NEI NIH HHS
Language: English
Date published: 09/01/2014
Academic Unit: Iowa Neuroscience Institute; Biochemistry and Molecular Biology; University College Courses; Ophthalmology and Visual Sciences
Record Identifier: 9984024522902771

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