ArticleProceedings of the National Academy of Sciences of the United States of America1992
Heterotrimeric G proteins in synaptoneurosome membranes are crosslinked by p-phenylenedimaleimide, yielding structures comparable in size to crosslinked tubulin and F-actin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 39 citations in OpenAlex.
- Oligomerization of G protein-coupled receptors: past, present, and future.Biochemistry · 2004Review
- Is signal transduction modulated by an interaction between heterotrimeric G-proteins and tubulin?Endocrine · 1997Review
- Close association of the alpha subunits of Gq and G11 G proteins with actin filaments in WRK1 cells: relation to G protein-mediated phospholipase C activation.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Signal transduction: evolution of an idea.Environmental health perspectives · 1995Review
- Characterization of caveolin-rich membrane domains isolated from an endothelial-rich source: implications for human disease.The Journal of cell biology · 1994Article
- Clustering and immobilization of acetylcholine receptors by the 43-kD protein: a possible role for dystrophin-related protein.The Journal of cell biology · 1993Article
- 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
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have treated rat brain synaptoneurosomes with the crosslinking agent N,N'-1,4-phenylenedimaleimide under conditions that cause extensive crosslinking of tubulin, F-actin, and the alpha and beta subunits of three major types of heterotrimeric GTP-binding regulatory proteins (G(o), Gs, Gi) present in brain membranes. The major crosslinked products are coeluted from Bio-Gel sizing columns as very large structures that do not penetrate stacking gels during SDS/PAGE. The alpha subunits but not the beta subunits of Gs, G(o) and Gi also yield crosslinked products of intermediate sizes. None of the products are as small as the heterotrimeric G proteins extracted from brain by cholate or Lubrol. However, the large and intermediate crosslinked structures are strikingly similar to the large, polydisperse structures of the alpha subunits of Gs, Gi, and G(o) extracted from synaptoneurosomes by the detergent octyl glucoside, which have sedimentation properties of multimeric proteins. Several ways in which multimeric forms of G proteins can explain the dynamic and pleiotropic actions of hormones and GTP on signal-transducing systems are discussed.
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