A role for rhodopsin in a signal transduction cascade that regulates membrane trafficking and photoreceptor polarity
Open accessAbstract
This review summarizes the most recent progress in the understanding of the role of rhodopsin C-terminal domain in the regulation of intracellular trafficking and photoreceptor morphogenesis. A proposed cascade of molecular interactions, initiated by the rhodopsin C-terminal sequence VXPX-COOH during trafficking from the Golgi/TGN in retinal photoreceptors, is relayed by the small GTPase ARF4 to the downstream effectors. One of the candidates for an ARF4 effector is the ARF-GAP ASAP1, which may function as a subunit of, or form a novel protein coat involved in trafficking from the TGN and in cytoskeletal remodeling, whose assembly is regulated by the binding of ARF4 to rhodopsin, and whose function is essential for the polarized trafficking toward the ROS.
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ASAP1 is a GAP that forms a complex with Arf4 and regulates GTP hydrolysis for Arf1, Arf4, and Arf5.
“ASAP1, a GAP that was previously shown to form a complex with Arf4 and regulate GTP hydrolysis for Arf1, Arf4, and Arf5 [32], [33].”
From Arf4 Determines Dentate Gyrus-Mediated Pattern Separation by Regulating Dendritic Spine Development (2012) · cites this paper as [33]
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Arf4 Determines Dentate Gyrus-Mediated Pattern Separation by Regulating Dendritic Spine Development
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- Authors
- Deretic, D.
- Affiliations
- University of New Mexico (US)
- Corresponding author
- Deretic, Dusanka
- ORCID
- Deretic, Dusanka
- Venue
- Vision Research
- Publisher
- Elsevier BV
- Published
- 2006-12
- Volume
- 46
- Issue
- 27
- Pages
- 4427-4433
- ISSN
- 0042-6989 (ISSN-L)
- OpenAlex
- W2029862966
- Cited by
- 86
- References
- 0
- Citations by year
- 2024: 1 · 2023: 2 · 2021: 5 · 2020: 3 · 2019: 2 · 2018: 2 · 2017: 4 · 2016: 3 · 2015: 2 · 2014: 4 · 2013: 7 · 2012: 8
- FWCI
- 0.74
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Vision Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Eye Institute (R01EY012421, EY-12421)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinal Development and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- rhodopsin, C-terminal domain, signal transduction, membrane trafficking, ARF4, ASAP1, ArfGAP, retinal outer segments, cytoskeletal remodeling
- MeSH terms
- Animals, Cell Membrane, Humans, Mutation, Rhodopsin, Rod Cell Outer Segment, Vision, Ocular, Cell Polarity, Protein Structure, Tertiary, Neurodegenerative Diseases, Protein Transport
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