ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2013
Phosducin-like protein 1 is essential for G-protein assembly and signaling in retinal rod photoreceptors.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Mapping the chaperonin TRiC/CCT interactome in mouse photoreceptors reveals functional significance for energy metabolism.PloS one · 2026Article
- Protein folding by the CCT/TRiC chaperone complex.Current opinion in structural biology · 2025Review
- Compound heterozygous mutations in a mouse model of Leber congenital amaurosis reveal the role of CCT2 in photoreceptor maintenance.Communications biology · 2024Article
- Germline knockout ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Visualizing the chaperone-mediated folding trajectory of the G protein β5 β-propeller.Molecular cell · 2023Article
- Transducin Partners Outside the Phototransduction Pathway.Frontiers in cellular neuroscience · 2020Article
- CCT2 Mutations Evoke Leber Congenital Amaurosis due to Chaperone Complex Instability.Scientific reports · 2016Article
- Article
- Structures of the Gβ-CCT and PhLP1-Gβ-CCT complexes reveal a mechanism for G-protein β-subunit folding and Gβγ dimer assembly.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Retinal cone photoreceptors require phosducin-like protein 1 for G protein complex assembly and signaling.PloS one · 2015Article
- Membrane protein transport in photoreceptors: the function of PDEδ: the Proctor lecture.Investigative ophthalmology & visual science · 2014Article
- Essential role of the chaperonin CCT in rod outer segment biogenesis.Investigative ophthalmology & visual science · 2014Article
- Programmed cell death protein 5 interacts with the cytosolic chaperonin containing tailless complex polypeptide 1 (CCT) to regulate β-tubulin folding.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
G-protein β subunits perform essential neuronal functions as part of G-protein βγ and Gβ5-regulators of G-protein signaling (RGS) complexes. Both Gβγ and Gβ5-RGS are obligate dimers that are thought to require the assistance of the cytosolic chaperonin CCT and a cochaperone, phosducin-like protein 1 (PhLP1) for dimer formation. To test this hypothesis in vivo, we deleted the Phlp1 gene in mouse (Mus musculus) retinal rod photoreceptor cells and measured the effects on G-protein biogenesis and visual signal transduction. In the PhLP1-depleted rods, Gβγ dimer formation was decreased 50-fold, resulting in a >10-fold decrease in light sensitivity. Moreover, a 20-fold reduction in Gβ5 and RGS9-1 expression was also observed, causing a 15-fold delay in the shutoff of light responses. These findings conclusively demonstrate in vivo that PhLP1 is required for the folding and assembly of both Gβγ and Gβ5-RGS9.
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Registered trials
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