Ultrastructural localization of the GTP-binding protein Go in neurons

Gabrion, Jacqueline; Brabet, Philippe; Dao, Benjamin; Homburger, Vincent; Dumuis, Aline; Sebben, Michèle; Rouot, Bruno; Bockaert, Joël

doi:10.1016/0898-6568(89)90025-9

Cited by 46 publications

(28 citation statements)

References 37 publications

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“…Go protein was principally found on the cytoplasmic face of the plasma membrane lining the cell body and the neurites, especially at 'cell-to-cell' contacts. Go was also detected in the cytoplasmic matrix, between the endoplasmic reticulum and Golgi cisternae [70] . These findings strongly suggest that the Go protein is involved in transducing chemical signals at the synaptic level and likely modulates synaptic functions by controlling the activity of effectors localized away from the synaptic membrane.…”

Section: Go Expression Patternmentioning

confidence: 97%

Molecular Mechanisms of Go Signaling

2009

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Go is the most abundant G protein in the central nervous system, where it comprises about 1% of membrane protein in mammalian brains. It functions to couple cell surface receptors to intercellular effectors, which is a critical process for cells to receive, interpret and respond to extracellular signals. Go protein belongs to the pertussis toxin-sensitive Gi/Go subfamily of G proteins. A number of G-protein-coupled receptors transmit stimuli to intercellular effectors through Go. Go regulates several cellular effectors, including ion channels, enzymes, and even small GTPases to modulate cellular function. This review summarizes some of the advances in Go research and proposes areas to be further addressed in exploring the functional role of Go.

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Section: Go Expression Patternmentioning

confidence: 97%

Molecular Mechanisms of Go Signaling

2009

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“…Their association with the plasma membrane allows them to interact with both membrane receptors and effectors [Gilman, 19871. Recently several groups have shown that these peptides are associated with various cellular organelles and not solely confined to the plasma membranes [Brabet et al, 1988;Gabrion et al, 1989;Wanget al, 1989;Ercolani et al, 1990;Lewis et al, 1991;Muntz et al, 1992;Stow and Dealmeida, 1993;Saffriz et al, 1994;Wilson et al, 19941. We also found that in cultured adipocytes Cadrin et al, 19931, G,a was mainly localized in cytoplasmic vesicular structures and in the nucleus, with F-actin, and the Golgi apparatus and Gia3 was associated with the Golgi apparatus.…”

Section: Ntrodu Cti 0 Nmentioning

confidence: 98%

Comparison of the subcellular distribution of G-proteins in hepatocytes in situ and in primary cultures

et al. 1996

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The subcellular localization of the heterotrimeric G-proteins in hepatocytes in situ was compared to that in hepatocytes in primary culture. The ability of various ligands to activate adenylyl cyclase (AC) in membrane preparations was also investigated. In hepatocytes in situ the G proteins were mainly localized at the plasma membrane while in hepatocytes in culture they were predominantly cytoplasmic. The localization of the G-proteins in hepatocytes in situ correlates with their role in signal transduction. In homogenates prepared from the cultured cells, ligands which stimulate AC via Gs alpha were without effect, which was consistent with the localization of Gs alpha in the cytoplasmic and nuclear compartments. The "relocalization" of the G proteins to the cytoplasm when cells are cultured suggests that transmembrane signalling may be regulated by cell differentiation and cell-cell and cell-extracellular matrix interactions.

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“…Examination of the location of G protein tl subunits, by either immunoblotting subcellular fractions from various cells (Rotrosen et al, 1988;Bokoch et al, 1988;Ali et al, 1989) or by use of immunocytochemistry (Gabrion et al, 1989), has indicated a more varied location that might be anticipated from their known function. As well as being associated with plasma membranes, G proteins have been detected in various microsomal fractions and indeed in cytoplasm (Ransnas and Insel, 1988b).…”

Section: Discussionmentioning

confidence: 99%

Plasma‐membrane‐independent pool of the α subunit of the stimulatory guanine‐nucleotide‐binding regulatory protein in a low‐density‐membrane fraction of S49 lymphoma cells

Svoboda¹,

Kvapil²,

Insel³

et al. 1992

European Journal of Biochemistry

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We report that compartmentalisation of the stimulatory guanine‐nucleotide‐binding regulatory protein (Gs) exists in S49 lymphoma cells. In addition to the previously reported cytosolic form of the α subunit of Gs (Gsα) [Ransnäs, L. A., Svoboda P., Jasper, J. R. & Insel, P. A. (1989) Proc. Natl Acad. Sci. USA 86, 7900–7903], three membrane‐bound forms of Gsα were identified through ratezonal centrifugation in sucrose density gradients, Gsα‐specific anti‐peptide serum and an adenylate cyclase complementation assay. The sedimentation profile of the first pool of Gsα in the high‐density portion of the gradient (1.13–1.16 g/cm3) is identical with that of β‐adrenergic‐receptor binding, Na/K‐ATPase and adenylate cyclase activity, and may therefore be identified as plasma‐membrane fragments. The second pool, which was recovered in the middle portion of the gradient (1.09–1.11 g/cm3), contains a much lower total amount of Gsα and correlates with the endoplasmic reticulum (microsomal) enzyme markers, NADPH–cytochrome‐c reductase and glucose‐6‐phosphatase. The identity of the third pool of Gsα located at the top of the gradient (1.06–1.08 g/cm3), is unknown. The Golgi apparatus marker, UDPgalactose:N‐acetylglucosamine glycosyltransferase, was partially recovered in this area; however, this enzyme was also present in the high‐density portion of the gradient. Complete absence of specific adenylate cyclase and Na/K‐ATPase activity indicates that this low‐density (light) membrane form of Gsα is distinct from any plasma‐membrane fragments. Furthermore, sedimentation at 100000 ×g proves its particulate (membrane) character. The light membrane form of Gsα subunit is functionally active in an adenylate cyclase complementation assay using cyc− membranes devoid of Gsα. Overall, our data indicates that a substantial portion of Gsα is localized in membrane pools other than plasma membrane.

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Ultrastructural localization of the GTP-binding protein Go in neurons

Cited by 46 publications

References 37 publications

Molecular Mechanisms of Go Signaling

Molecular Mechanisms of Go Signaling

Comparison of the subcellular distribution of G-proteins in hepatocytes in situ and in primary cultures

Plasma‐membrane‐independent pool of the α subunit of the stimulatory guanine‐nucleotide‐binding regulatory protein in a low‐density‐membrane fraction of S49 lymphoma cells

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