Purification of the G-protein G13 from rat brain membranes

Harhammer, Rainer; Nürnberg, Bernd; Spicher, Karsten; Schultz, Günter

doi:10.1042/bj3030135

Cited by 14 publications

(19 citation statements)

References 43 publications

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“…Membranes from bovine brains were prepared as described [20], and proteins were solubilized with 1% Na-cholate. Heterotrimeric Gi/Go proteins were isolated by consecutive chromatographic steps on DEAE-Sepharose Fast Flow (Pharmacia), Ultrogel AcA-34 (Serva) and heptylamine-Sepharose [21].…”

Section: Z2 Purification Of G~'~ Dimersmentioning

confidence: 99%

“…Subsequently, the beads were washed six times with buffer A and eluted three times with buffer B. Eluate and wash fractions were collected and subjected to SDS-PAGE performed on 10% acrylamide gels according to Laemmli [24]. Blotting of proteins separated by SDS-PAGE and immunological detection of filter-bound proteins using antiserum AS 11 (anti-[5 ........... ) and the enhanced chemiluminescence Western blotting (ECL) system (Amersham) were carried out as described previously [20,25].…”

Section: Complex Formation Of Gst-rho With G[57mentioning

confidence: 99%

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Interaction of G protein Gβγ dimers with small GTP‐binding proteins of the Rho family

1996

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GIlt/dimers of heterotrimeric G proteins have been shown to be important for the translocation of cytosolic proteins t. membranes. The involvement of G~/ in those signaling processes mediated by small GTP-binding proteins of the Rho family was studied using purified proteins. We showed specific binding of bovine brain Gl~f to immobilized GST-Rho fusion proteins. In addition, brain G[~, but not transducin G[~, was able to inhibit GTPyS binding to GST-Rho in a concentrationdependent manner. GTP3~S binding to GST-Rac was also decreased by brain G[]q, whereas nucleotide binding to GSTCdc42 was not changed. We conclude that G[]q, dimers may participate in the process of membrane attachment and/or other regulations of Rho and Rac.

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Section: Z2 Purification Of G~'~ Dimersmentioning

confidence: 99%

Section: Complex Formation Of Gst-rho With G[57mentioning

confidence: 99%

Interaction of G protein Gβγ dimers with small GTP‐binding proteins of the Rho family

1996

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“…GI2 and G~3, belonging to the Gt2 subfamily, are expressed ubiquitously at very low abundance [70,71]. Native Go~3 and Go~t2 have recently been purified from rat and bovine brain membranes [72][73][74][75]. Their Get subunits share less than 50% amino acid identity than other G protein subfamilies.…”

Section: G(~ Subunitsmentioning

confidence: 99%

Receptors and G proteins as primary components of transmembrane signal transduction

1995

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Seven-transmembrane receptors signal through nucleotide-binding proteins (G proteins) into the cell. G proteins are membrane-associated proteins composed of three subunits termed alpha, beta and gamma, of which the G alpha subunit classifies the heterotrimer. So far, 23 different mammalian G alpha subunits are known, which are grouped in four subfamilies (Gs, Gi, Gq, G12) on the basis of their amino acid similarity. They carry an endogenous GTPase activity allowing reversible functional coupling between ligand-bound receptors and effectors such as enzymes and ion channels. In addition, five G beta and seven G gamma subunits have been identified which form tightly associated beta gamma heterodimers. Upon activation by a ligand-bound receptor the G protein dissociates into G alpha and G beta gamma, which both transmit signal by interacting with effectors. On the G protein level, specificity and selectivity of the incoming signal is accomplished by G protein trimers composed of distinct subunits. On the other hand, many receptors have been shown to activate different G proteins, thereby regulating diverse signal transduction pathways.

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“…Proteins for Western analysis were prepared from mouse brains (41). Samples were separated by SDS͞PAGE and blotted onto nitrocellulose membranes BA85 (Schleicher & Schüll).…”

Section: Methodsmentioning

confidence: 99%

Interaction of Gα ₁₂ with Gα ₁₃ and Gα _q signaling pathways

Müller

Mancino

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

113

127

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The G12 subfamily of heterotrimeric G-proteins consists of two members, G 12 and G13. Gene-targeting studies have revealed a role for G 13 in blood vessel development. Mice lacking the ␣ subunit of G 13 die around embryonic day 10 as the result of an angiogenic defect. On the other hand, the physiological role of G12 is still unclear. To address this issue, we generated G␣ 12-deficient mice. In contrast to the G␣ 13-deficient mice, G␣12-deficient mice are viable, fertile, and do not show apparent abnormalities. However, G␣ 12 does not seem to be entirely redundant, because in the offspring generated from G␣ 12؎ G␣13؎ intercrosses, at least one intact G␣12 allele is required for the survival of animals with only one G␣13 allele. In addition, G␣12 and G␣13 showed a difference in mediating cell migratory response to lysophosphatidic acid in embryonic fibroblast cells. Furthermore, mice lacking both G␣ 12 and G␣q die in utero at about embryonic day 13. These data indicate that the G␣ 12-mediated signaling pathway functionally interacts not only with the G␣ 13-but also with the G␣q/11-mediated signaling systems.

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Purification of the G-protein G13 from rat brain membranes

Cited by 14 publications

References 43 publications

Interaction of G protein Gβγ dimers with small GTP‐binding proteins of the Rho family

Interaction of G protein Gβγ dimers with small GTP‐binding proteins of the Rho family

Receptors and G proteins as primary components of transmembrane signal transduction

Interaction of Gα ₁₂ with Gα ₁₃ and Gα _q signaling pathways

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Purification of the G-protein G13 from rat brain membranes

Cited by 14 publications

References 43 publications

Interaction of G protein Gβγ dimers with small GTP‐binding proteins of the Rho family

Interaction of G protein Gβγ dimers with small GTP‐binding proteins of the Rho family

Receptors and G proteins as primary components of transmembrane signal transduction

Interaction of Gα 12 with Gα 13 and Gα q signaling pathways

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Interaction of Gα ₁₂ with Gα ₁₃ and Gα _q signaling pathways