ArticleThe Journal of biological chemistry2012
Crystal structures of the scaffolding protein LGN reveal the general mechanism by which GoLoco binding motifs inhibit the release of GDP from Gαi.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Molecular insights into AGS3's role in spindle orientation: a biochemical perspective.Journal of molecular cell biology · 2025Article
- Liquid-liquid phase separation in hair cell stereocilia development and maintenance.Computational and structural biotechnology journal · 2023Review
- The Nuclear Mitotic Apparatus (NuMA) Protein: A Key Player for Nuclear Formation, Spindle Assembly, and Spindle Positioning.Frontiers in cell and developmental biology · 2021Review
- AGS3 and GαMolecules (Basel, Switzerland) · 2020Article
- Diversity of activator of G-protein signaling (AGS)-family proteins and their impact on asymmetric cell division across taxa.Developmental biology · 2020Review
- Ric-8A, a GEF, and a Chaperone for G Protein α-Subunits: Evidence for the Two-Faced Interface.BioEssays : news and reviews in molecular, cellular and developmental biology · 2020Article
- Intramolecular interaction in LGN, an adaptor protein that regulates mitotic spindle orientation.The Journal of biological chemistry · 2019Article
- Structural design principles that underlie the multi-specific interactions of GαScientific reports · 2019Article
- Article
- Identification of residues crucial for the interaction between human neuroglobin and the α-subunit of heterotrimeric Gi protein.Scientific reports · 2016Article
- Direct Coupling of a Seven-Transmembrane-Span Receptor to a Gαi G-Protein Regulatory Motif Complex.Molecular pharmacology · 2015Article
- Activators of G protein signaling exhibit broad functionality and define a distinct core signaling triad.Molecular pharmacology · 2014Review
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6 authors.
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Abstract
GoLoco (GL) motif-containing proteins regulate G protein signaling by binding to Gα subunit and acting as guanine nucleotide dissociation inhibitors. GLs of LGN are also known to bind the GDP form of Gα(i/o) during asymmetric cell division. Here, we show that the C-terminal GL domain of LGN binds four molecules of Gα(i)·GDP. The crystal structures of Gα(i)·GDP in complex with LGN GL3 and GL4, respectively, reveal distinct GL/Gα(i) interaction features when compared with the only high resolution structure known with GL/Gα(i) interaction between RGS14 and Gα(i1.) Only a few residues C-terminal to the conserved GL sequence are required for LGN GLs to bind to Gα(i)·GDP. A highly conserved "double Arg finger" sequence (RΨ(D/E)(D/E)QR) is responsible for LGN GL to bind to GDP bound to Gα(i). Together with the sequence alignment, we suggest that the LGN GL/Gα(i) interaction represents a general binding mode between GL motifs and Gα(i). We also show that LGN GLs are potent guanine nucleotide dissociation inhibitors.
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