ArticleProceedings of the National Academy of Sciences of the United States of America2001
Rethinking the role of phosducin: light-regulated binding of phosducin to 14-3-3 in rod inner segments.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. 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, 37 citations in OpenAlex.
- Structural insights into the functional roles of 14-3-3 proteins.Frontiers in molecular biosciences · 2022Review
- Analysis of 14-3-3 isoforms expressed in photoreceptors.Experimental eye research · 2018Article
- iTRAQ Quantitative Proteomic Analysis of Vitreous from Patients with Retinal Detachment.International journal of molecular sciences · 2018Article
- Structural Basis for the 14-3-3 Protein-Dependent Inhibition of Phosducin Function.Biophysical journal · 2017Article
- Structural Characterization of Phosducin and Its Complex with the 14-3-3 Protein.The Journal of biological chemistry · 2015Article
- Functional EF-hands in neuronal calcium sensor GCAP2 determine its phosphorylation state and subcellular distribution in vivo, and are essential for photoreceptor cell integrity.PLoS genetics · 2014Article
- Article
- Structural modulation of phosducin by phosphorylation and 14-3-3 protein binding.Biophysical journal · 2012Article
- Phosphorylation of phosducin accelerates rod recovery from transducin translocation.Investigative ophthalmology & visual science · 2012Article
- The physiological roles of phosducin: from retinal function to stress-dependent hypertension.Cellular and molecular life sciences : CMLS · 2011Review
- Phosducin regulates transmission at the photoreceptor-to-ON-bipolar cell synapse.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Phosphorylation of GRK7 by PKA in cone photoreceptor cells is regulated by light.Journal of neurochemistry · 2008Article
- Light-induced translocation of cyclic-GMP phosphodiesterase on rod disc membranes in rat retina.Molecular vision · 2008Article
- Function of phosducin-like proteins in G protein signaling and chaperone-assisted protein folding.Cellular signalling · 2007Review
- Phosducin regulates the expression of transducin betagamma subunits in rod photoreceptors and does not contribute to phototransduction adaptation.The Journal of general physiology · 2007Article
- Photic regulation of arylalkylamine N-acetyltransferase binding to 14-3-3 proteins in retinal photoreceptor cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- Is Melanoma a stem cell tumor? Identification of neurogenic proteins in trans-differentiated cells.Journal of translational medicine · 2005Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Phosducin (Pd), a small protein found abundantly in photoreceptors, is widely assumed to regulate light sensitivity in the rod outer segment through interaction with the heterotrimeric G protein transducin. But, based on histochemistry and Western blot analysis, Pd is found almost entirely in the inner segment in both light and dark, most abundantly near the rod synapse. We report a second small protein, 14-3-3, in the rod with a similar distribution. By immunoprecipitation, phospho-Pd is found to interact with 14-3-3 in material from dark-adapted retina, and this interaction is markedly diminished by light, which dephosphorylates Pd. Conversely, unphosphorylated Pd binds to inner segment G protein(s) in the light. From these results and reported functions of 14-3-3, we have constructed a hypothesis for the regulation of light sensitivity at the level of rod synapse. By dissociating the Pd/14-3-3 complex, light enables both proteins to function in this role.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.