ArticleThe EMBO journal1997
A small region in phosducin inhibits G-protein betagamma-subunit function.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 41 citations in OpenAlex.
- Development of inhibitors of heterotrimeric Gαi subunits.Bioorganic & medicinal chemistry · 2014Article
- Cell type influences the molecular mechanisms involved in hormonal regulation of ERG K+ channels.Pflugers Archiv : European journal of physiology · 2012Article
- Regulators of G-protein signalling in Fusarium verticillioides mediate differential host-pathogen responses on nonviable versus viable maize kernels.Molecular plant pathology · 2011Article
- 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
- The phosducin-like protein PhnA is required for Gbetagamma-mediated signaling for vegetative growth, developmental control, and toxin biosynthesis in Aspergillus nidulans.Eukaryotic cell · 2006Article
- Phosducin-like proteins in Dictyostelium discoideum: implications for the phosducin family of proteins.The EMBO journal · 2003Article
- Effects of two Gbetagamma-binding proteins--N-terminally truncated phosducin and beta-adrenergic receptor kinase C terminus (betaARKct)--in heart failure.Gene therapy · 2003Article
- Identification of bdm-1, a gene involved in G protein beta-subunit function and alpha-subunit accumulation.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Structural features of heterotrimeric G-protein-coupled receptors and their modulatory proteins.Molecular neurobiology · 1999Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
G-protein betagamma-subunits (G(betagamma)) are active transmembrane signalling components. Their function recently has been observed to be regulated by the cytosolic protein phosducin. We show here that a small fragment (amino acids 215-232) contained in the C-terminus of phosducin is sufficient for high-affinity interactions with G(betagamma). Corresponding peptides not only disrupt G(betagamma)-G(alpha) interactions, as defined by G(betagamma)-stimulated GTPase activity of alpha(o), but also other G(betagamma)-mediated functions. The NMR structure of a peptide encompassing this region shows a loop exposing the side chains of Glu223 and Tyr224, and peptides with a substitution of either of these amino acids show a complete loss of activity towards G(o). Mutation of this Tyr224 to Ala in full-length phosducin reduced the functional activity of phosducin to that of phosducin's isolated N-terminus, indicating the importance of this residue within the short, structurally defined C-terminal segment. This small peptide derived from phosducin, may represent a model of a G(betagamma) inhibitor, and illustrates the potential of small compounds to affect G(betagamma) functions.
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