ArticleProceedings of the National Academy of Sciences of the United States of America1990
Octyl glucoside extracts GTP-binding regulatory proteins from rat brain "synaptoneurosomes" as large, polydisperse structures devoid of beta gamma complexes and sensitive to disaggregation by guanine nucleotides.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 46 citations in OpenAlex.
- Analysis of the N-terminal binding domain of Go alpha.The Biochemical journal · 1997Article
- Is signal transduction modulated by an interaction between heterotrimeric G-proteins and tubulin?Endocrine · 1997Review
- N-terminal binding domain of Galpha subunits: involvement of amino acids 11-14 of Galphao in membrane attachment.The Biochemical journal · 1997Article
- Distinct biochemical properties of the native members of the G12 G-protein subfamily. Characterization of G alpha 12 purified from rat brain.The Biochemical journal · 1996Article
- Modulation of the hepatic alpha 1-adrenoceptor responsiveness by colchicine: dissociation of free cytosolic Ca(2+)-dependent and independent responses.British journal of pharmacology · 1996Article
- Signal transduction: evolution of an idea.Environmental health perspectives · 1995Review
- The disaggregation theory of signal transduction revisited: further evidence that G proteins are multimeric and disaggregate to monomers when activated.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Heterotrimeric G proteins in synaptoneurosome membranes are crosslinked by p-phenylenedimaleimide, yielding structures comparable in size to crosslinked tubulin and F-actin.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- Amino acids 367-376 of the Gs alpha subunit induce membrane association when fused to soluble amino-terminal deleted Gi1 alpha subunit.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
- Glucagon induces disaggregation of polymer-like structures of the alpha subunit of the stimulatory G protein in liver membranes.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
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2 authors at 1 institution in 1 country.
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Abstract
GTP-binding regulatory proteins are generally purified from cholate-extracted membranes in the form of heterotrimers (G proteins) consisting of a GTP-binding subunit (alpha protein) complexed with a tightly interacted heterodimer termed beta gamma. In this study we extracted the proteins from rat brain "synaptoneurosomes" using the neutral detergent 1-octyl beta-D-glucopyranoside (octyl glucoside). Using specific antibodies for detection by immunoblotting and sucrose gradients for analyzing hydrodynamic properties, we found that each species of alpha protein (alpha subunits of stimulatory, inhibitory, and brain GTP-binding proteins) exhibited a broad range (4 S to greater than 12 S) of polydisperse structures with peak values (5 S to 7 S) considerably greater than that of heterotrimeric G proteins. The beta subunit proteins, for example, appeared as a homogeneous peak at 4.4 S within which only a fraction of the total alpha proteins can be associated. Incubation of octyl glucose extracts at 30 degrees C rapidly sedimented the alpha proteins but not the beta proteins. Incubation at 30 degrees C with guanosine 5'[gamma-thio]triphosphate (10-100 microM) prevented rapid sedimentation. Hydrodynamic analysis revealed that all alpha proteins were converted to approximately 4 S structures by the actions of guanosine 5'-[gamma-thio]triphosphate without change in the hydrodynamic properties of the beta proteins. Extraction of the membranes with sodium cholate instead of octyl glucoside resulted in complete loss of the large, polydisperse structures of the alpha proteins; the S values were approximately 4 S, in the range for beta proteins. These findings suggest that the transducing GTP-binding proteins in synaptoneurosomes exist as polydisperse, possibly multimer, structures of various size that are stable in octyl glucoside but destroyed by cholate. The polydisperse structures are not associated with beta gamma complexes and are sensitive to the disaggregating effects of guanosine 5'-[gamma-thio]triphosphate.
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