ArticleCellular and molecular life sciences : CMLS2013
Light-dependent phosphorylation of Bardet-Biedl syndrome 5 in photoreceptor cells modulates its interaction with arrestin1.
Article in Cellular and molecular life sciences : CMLS, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 32 citations in OpenAlex.
- Characterization of Usher Syndrome Type 2-Associated Proteins in the Retina via Affinity Purification-Mass Spectrometry.Molecular & cellular proteomics : MCP · 2026Article
- Cellular and Molecular Mechanisms of Pathogenesis Underlying Inherited Retinal Dystrophies.Biomolecules · 2023Review
- Retinal Degeneration Animal Models in Bardet-Biedl Syndrome and Related Ciliopathies.Cold Spring Harbor perspectives in medicine · 2023Review
- Loss of the Bardet-Biedl protein Bbs1 alters photoreceptor outer segment protein and lipid composition.Nature communications · 2022Article
- Structure and dynamics of photoreceptor sensory cilia.Pflugers Archiv : European journal of physiology · 2021Review
- On the Wrong Track: Alterations of Ciliary Transport in Inherited Retinal Dystrophies.Frontiers in cell and developmental biology · 2021Review
- BBSome Component BBS5 Is Required for Cone Photoreceptor Protein Trafficking and Outer Segment Maintenance.Investigative ophthalmology & visual science · 2020Article
- The myosin-tail homology domain of centrosomal protein 290 is essential for protein confinement between the inner and outer segments in photoreceptors.The Journal of biological chemistry · 2019Article
- Defining the layers of a sensory cilium with STORM and cryoelectron nanoscopy.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Rescue of M-cone Function in Aged Opn1mw-/- Mice, a Model for Late-Stage Blue Cone Monochromacy.Investigative ophthalmology & visual science · 2019Article
- BBSome trains remove activated GPCRs from cilia by enabling passage through the transition zone.The Journal of cell biology · 2018Article
- Bardet-Biedl syndrome-8 (BBS8) protein is crucial for the development of outer segments in photoreceptor neurons.Human molecular genetics · 2018Article
- Structural and molecular bases of rod photoreceptor morphogenesis and disease.Progress in retinal and eye research · 2016Review
- Intracellular localization of α-tubulin acetyltransferase ATAT1 in rat ciliated cells.Medical molecular morphology · 2016Article
- Loss of the BBSome perturbs endocytic trafficking and disrupts virulence of Trypanosoma brucei.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A Splice Variant of Bardet-Biedl Syndrome 5 (BBS5) Protein that Is Selectively Expressed in Retina.PloS one · 2016Article
- Arrestin 1 and Cone Arrestin 4 Have Unique Roles in Visual Function in an All-Cone Mouse Retina.Investigative ophthalmology & visual science · 2015Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Arrestins are dynamic proteins that move between cell compartments triggered by stimulation of G-protein-coupled receptors. Even more dynamically in vertebrate photoreceptors, arrestin1 (Arr1) moves between the inner and outer segments according to the light conditions. Previous studies have shown that the light-driven translocation of Arr1 in rod photoreceptors is initiated by rhodopsin through a phospholipase C/protein kinase C (PKC) signaling cascade. The purpose of this study is to identify the PKC substrate that regulates the translocation of Arr1. Mass spectrometry was used to identify the primary phosphorylated proteins in extracts prepared from PKC-stimulated mouse eye cups, confirming the finding with in vitro phosphorylation assays. Our results show that Bardet-Biedl syndrome 5 (BBS5) is the principal protein phosphorylated either by phorbol ester stimulation or by light stimulation of PKC. Via immunoprecipitation of BBS5 in rod outer segments, Arr1 was pulled down; phosphorylation of BBS5 reduced this co-precipitation of Arr1. Immunofluorescence and immunoelectron microscopy showed that BBS5 principally localizes along the axonemes of rods and cones, but also in photoreceptor inner segments, and synaptic regions. Our principal findings in this study are threefold. First, we demonstrate that BBS5 is post-translationally regulated by phosphorylation via PKC, an event that is triggered by light in photoreceptor cells. Second, we find a direct interaction between BBS5 and Arr1, an interaction that is modulated by phosphorylation of BBS5. Finally, we show that BBS5 is distributed along the photoreceptor axoneme, co-localizing with Arr1 in the dark. These findings suggest a role for BBS5 in regulating light-dependent translocation of Arr1 and a model describing its role in Arr1 translocation is proposed.
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