Functional domains of rhodopsin

Litman, Burton J.; Aton, B.; Hartley, Jonathan

doi:10.1016/0042-6989(82)90206-1

Cited by 57 publications

(7 citation statements)

References 12 publications

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“…The amino-terminus, which has no signal sequence, always contains sites for Nlinked glycosylation; the carboxy-terminus has typical sites for phosphorylation by protein kinase A and other kinases. Seven stretches of 22 -28 hydrophobic conserved residues, separated by hydrophilic segments, are found in each of the members of the family of proteins, as had been seen earlier in the well characterized rhodopsins which are also coupled to a GTP binding protein, transducin (Littman et al, 1982). This similarity has led to the suggestion that these receptors, which we propose to designate as 'R7G', share with bacteriorhodopsin its peculiar membrane topology (Fig.…”

Section: Structural Propertiesmentioning

confidence: 89%

Structure/function relationship of proteins belonging to the family of receptors coupled to GTP‐binding proteins

Strosberg

1991

European Journal of Biochemistry

236

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The structural properties of a number of proteins belonging to the family of receptors coupled to GTP binding proteins are discussed in relation to their function.The structure of the ligand binding site and of the regions involved in coupling to the G proteins are analyzed mainly for the adrenergic and muscarinic cholinergic receptors, for which site-directed mutagenesis and chimaeric constructions have been studied. The structure of the genes are compared and the presence of various regulatory elements is discussed in relation to control of expression.Mechanism of desensitization and internalization, while mostly studied for the j2-adrenergic receptor, are proposed to be generally applicable to all G-protein-coupled receptors.A wide variety of membrane receptors for hormones and neurotransmitters are coupled to guanine-nucleotide-binding regulatory 'G' proteins, which upon activation by receptors, stimulate or inhibit various effectors such as enzymes or ion channels. Among the family of receptors coupled to G proteins are those for adrenaline and other catecholamines, the 'adrenergic receptors' and those for acetylcholine and related muscarinic ligands, the 'muscarinic cholinergic' receptors. Other similar proteins belonging to this growing family are those for serotonine, for dopamine, for the tachykinins, and for the pituitary glycoprotein hormones, to mention but a few (Table 1).Several subtypes of these receptors have been defined on the basis of pharmacologic properties and more have been found recently through cloning of homologous genes. Expression of individual receptor subtypes in cells initially devoid of receptors reveal characteristic ligand-binding profiles and activation of different intracellular effector systems. The p1-, j2-and j3-adrenergic, the 5HT-1A serotoninergic (5HT = 5-hydroxytryptamine) and the D1 dopaminergic receptors through activation of a G, (GTP binding stimulatory) protein stimulate the membrane-bound adenylyl cyclase, leading to an increased production of cyclic AMP. The a2A-and a2B- Abbreviations. PAR, /I-adrenergic receptor; E-R7G, family of receptors having seven transmembrane domains, coupled to GTP binding proteins and having an extra long (= 333 residues) extracellular domain; G proteins, GTP binding regulatory proteins (G, = inhibitory, G, = stimulatory, G, = coupled to phospholipase); GRE, glucocorticoid responsive elements; 5HT, 5-hydroxytryptamine; m, muscarinic; R7G, family of receptors having seven transmembrane domains and coupled to GTP binding proteins. adrenergic, the m2 and m4 muscarinic cholinergic, the D2 dopaminergic receptors, through activation of a Gi (GTP binding inhibitory) protein, inhibit this cyclase, whereas the El-adrenergic, the m l , m3 and m5 muscarinic and the 5HT-1C and 5HT-2 serotoninergic receptors through coupling either to a Gi or a Go (GTP binding, coupled to other effectors) protein modulate the hydrolysis of polyphosphoinositol lipids by phospholipase A2 or C leading to the production of two second messengers, inositol tri(tetra)phosp...

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Section: Structural Propertiesmentioning

confidence: 89%

Structure/function relationship of proteins belonging to the family of receptors coupled to GTP‐binding proteins

Strosberg

1991

European Journal of Biochemistry

236

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“…In rhodopsin, proteolytic digestion of the third intracellular loop inhibits light-dependent coupling to the G protein transducin (43), and activation of the retinal phosphodiesterase (44). By analogy, the putative intracellular domains of the f32AR were predicted to interact with the G protein G •.…”

Section: Hydrophilic Intracellular Domains-receptor Regions Involved mentioning

confidence: 99%

Mutagenesis of the beta2-Adrenergic Receptor: How Structure Elucidates Function

Ostrowski

Kjelsberg²,

Caron³

et al. 1992

Annu. Rev. Pharmacol. Toxicol.

183

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“…Both the third cytoplasmic loop and the amino terminal region of the carboxy tail of rhodopsin have been directly implicated in rhodopsin transducin coupling (Takemoto et al 1985, Littman et al 1982. Two mutations in the carboxy terminal region of the third cytoplasmic loop of the human fJ2-AR, one involving a deletion of seven amino acids and the other a substitution of four amino acids (Figure 3), each caused a marked decrease in agonist dependent adenylyl cyclase activation ( Figure 5).…”

Section: Carboxy Tail and Cytoplasmic Regionsmentioning

confidence: 99%

Structure Of The Adrenergic And Related Receptors

O'dowd¹

1989

Annual Review of Neuroscience

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Functional domains of rhodopsin

Cited by 57 publications

References 12 publications

Structure/function relationship of proteins belonging to the family of receptors coupled to GTP‐binding proteins

Structure/function relationship of proteins belonging to the family of receptors coupled to GTP‐binding proteins

Mutagenesis of the beta2-Adrenergic Receptor: How Structure Elucidates Function

Structure Of The Adrenergic And Related Receptors

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