Structure and Function of G-Protein βγ Subunit

Neer, Eva J.

doi:10.1016/b978-0-12-377450-7.50007-1

Cited by 9 publications

(3 citation statements)

References 71 publications

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“…'t and can be analyzed by sucrose density centrifugation only in the presence of detergents [27]. Some of these dimers bind large quantities of detergent [28]. It is thus not too surprising that their sedimentation behaviour is markedly dependent on the type of detergent used [29].…”

Section: Resultsmentioning

confidence: 99%

Expression, characterization and purification of soluble G‐protein βγ dimers composed of defined subunits in baculovirus‐infected insect cells

et al. 1992

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Recombinant β1γ2 dimers of signal‐transducing guanine nucleotide‐binding proteins (G‐proteins) carrying a mutation known to block isoprenylation of the γ2 subunit were expressed as a soluble protein in baculovirus‐infected insect cells. The soluble βγ dimer was analyzed by sucrose density gradient centrifugation and purified to near homogeneity in the absence of detergents. The sedimentation velocity studies gave an s 20,w value of 4.1 ± 0.4 S. The two subunits segregated as a dimer upon sucrose density gradient centrifugation and purification by sequential ion exchange and hydroxylapatite chromatography. The results show that baculovirus‐infected insect cells can be employed for high level production of pure G‐protein βγ dimers suitable for functional and structural characterization.

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Section: Resultsmentioning

confidence: 99%

Expression, characterization and purification of soluble G‐protein βγ dimers composed of defined subunits in baculovirus‐infected insect cells

et al. 1992

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“…It has been estimated that about 80 percent of currently identified primary messengers, including hormones, neurotransmitters, neuromodulators, and cellular activating factors, elicit their respective cellular responses through receptors which couple to G proteins (Birnbaumer et al, 1990a). Structurally G proteins are comprised of a (at least 20 isotypes, 39-52 kDa), p (4 isotypes identified to date, 35-37 kDa), and y (4 identified isotypes, 5-10 kDa) subunits, which have been purified andor cloned and, in a number of cases, for which the chromosomal loci of the respective genes have been determined (Birnbaumer et al, 1990a;Blatt et al, 1988;Heideman and Bourne, 1990;Neer and Clapham, 1990;Simon et al, 1991). These basic structural units are instrumental to the function of the G proteins.…”

Section: Cns Receptor Coupling and Signal Transductionmentioning

confidence: 99%

CNS signal transduction in the pathophysiology and pharmacotherapy of affective disorders and schizophrenia

Hudson

Lee

et al. 1993

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146

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Until recently, research on the neurochemical basis of affective disorders (AD) and schizophrenia (SCZ) focused on detecting postulated disturbances in presynaptic neurotransmitter release and metabolism, or postsynaptic receptor function. New insights into the molecular mechanisms involved in the propagation of neurotransmitter signals across biological membranes and in the regulation of neuronal responses have allowed the development of novel hypotheses, which may explain the altered postsynaptic neuroreceptor responsivity thought to be integral to the pathophysiology of these disorders. In this review we evaluate evidence from both basic science and clinical research implicating disturbances in postreceptor signal transduction in the pathophysiology and pharmacotherapy of AD and SCZ. Specific findings regarding potential postreceptor sites of pathophysiology are highlighted in each of these disorders, together with the growing body of data on the possible postreceptor loci of psychotropic drug action, especially lithium and antidepressants.

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“…It is also conceivable that the G␤␥ inactivating effect of the C terminus of this receptor may be affected by the amount of free G␤␥ inside the cell. There may be an intracellular free G␤␥ pool with different sizes in different cells (35). Excess G␤␥ may thus occupy the C terminus and attenuate its inhibitory effect.…”

Section: Lysmentioning

confidence: 99%

In Vivo Coupling of Insulin-like Growth Factor II/Mannose 6-Phosphate Receptor to Heteromeric G Proteins

Ikezu

Okamoto

Giambarella

et al. 1995

Journal of Biological Chemistry

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Structure and Function of G-Protein βγ Subunit

Cited by 9 publications

References 71 publications

Expression, characterization and purification of soluble G‐protein βγ dimers composed of defined subunits in baculovirus‐infected insect cells

Expression, characterization and purification of soluble G‐protein βγ dimers composed of defined subunits in baculovirus‐infected insect cells

CNS signal transduction in the pathophysiology and pharmacotherapy of affective disorders and schizophrenia

In Vivo Coupling of Insulin-like Growth Factor II/Mannose 6-Phosphate Receptor to Heteromeric G Proteins

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