How receptors talk to trimeric G proteins

https://doi.org/10.1016/S0955-0674(97)80054-3Get rights and content

Abstract

Stimulated by hormones and sensory stimuli, serpentine receptors promote the release of GDP that is bound to the α subunit of trimeric G proteins and its replacement by GTP. Recent investigations have begun to define the sizes, shapes, and relative orientations of receptors and G proteins, the surfaces through which they interact with one another, and conformational changes in both sets of molecules that underlie receptor-catalyzed guanine-nucleotide exchange.

References (66)

  • EA Dratz et al.

    NMR structure of a receptor-bound G-protein peptide

    Nature

    (1993)
  • BR Conklin et al.

    Substitution of three amino acids switches receptor specificity of Giα to that of Giα

    Nature

    (1993)
  • CD Strader et al.

    Structure and function of G protein-coupled receptors

    Annu Rev Biochem

    (1994)
  • T Namba et al.

    Alternative splicing of C-terminal tail of prostaglandin E receptor subtype EP3 determines G-protein specificity

    Nature

    (1993)
  • RL Gilchrist et al.

    The luteinizing hormone/chorionic gonadotropin receptor has distinct transmembrane conductors for cAMP and inositol phosphate signals

    J Biol Chem

    (1996)
  • CE Elling et al.

    Connectivity and orientation of the seven helical bundle in the tachykinin NK-1 receptor probed by zinc site engineering

    EMBO J

    (1996)
  • T Mizobe et al.

    Arrangement of transmembrane domains in adrenergic receptors. Similarity to bacteriorhodopsin

    J Biol Chem

    (1996)
  • ES Burstein et al.

    Structure—function of muscarinic receptor coupling to G proteins. Random saturation mutagenesis identifies a critical determinant of receptor affinity for G proteins

    J Biol Chem

    (1995)
  • T Iiri et al.

    Rapid GDP release from G in patients with gain and loss of endocrine function

    Nature

    (1994)
  • DG Lambright et al.

    The 2.0 Å crystal structure of a heterotrimeric G protein

    Nature

    (1996)
  • O Lichtarge et al.

    Evolutionarily conserved Gαβγ binding surfaces support a model of the G protein—receptor complex

    Proc Natl Acad Sci USA

    (1996)
  • BR Conklin et al.

    Structural elements of Gα subunits that interact with Gβγ, receptors, and effectors

    Cell

    (1993)
  • PD Garcia et al.

    Transducin-α C-terminal mutations present activation by rhodopsin: a new assay using recombinant proteins expressed in cultured cells

    EMBO J

    (1995)
  • CD Strader et al.

    The family of G-protein-coupled receptors

    FASEB J

    (1995)
  • GFX Schertler et al.

    Projection structure of rhodopsin

    Nature

    (1993)
  • GF Schertler et al.

    Projection structure of frog rhodopsin in two crystal forms

    Proc Natl Acad Sci USA

    (1995)
  • JM Baldwin

    The probable arrangement of the helices in G protein-coupled receptors

    EMBO J

    (1993)
  • BF O'Dowd et al.

    Palmitoylation of the human β2-adrenergic receptor

    J Biol Chem

    (1989)
  • PL Yeagle et al.

    Structure determination of the fourth cytoplasmic loop and carboxyl terminal domain of bovine rhodopsin

    Mol Vision

    (1996)
  • SR Coughlin

    Expanding horizons for receptors coupled to G proteins: diversity and disease

    Curr Opin Cell Biol

    (1994)
  • LA Price et al.

    Functional coupling of a mammalian somatostatin receptor to the yeast pheromone response pathway

    Mol Cell Biol

    (1995)
  • D Fu et al.

    Residues in the seventh membrane-spanning segment of the dopamine D2 receptor accessible in the binding-site crevice

    Biochemistry

    (1996)
  • CP Govardhan et al.

    Active site-directed inactivation of constitutively active mutants of rhodopsin

    J Biol Chem

    (1994)
  • Cited by (532)

    • Regulation of G Protein βγ Signaling

      2018, International Review of Cell and Molecular Biology
    View all citing articles on Scopus
    View full text