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Scaffolding proteins in G-protein signaling.

Andreeva AV, Kutuzov MA, Voyno-Yasenetskaya TA - J Mol Signal (2007)

Bottom Line: A number of scaffolding proteins have been identified that regulate various facets of GPCR signaling.In this review, we summarize current knowledge concerning those scaffolding proteins that are known to directly bind heterotrimeric G proteins, and discuss the composition of the protein complexes they assemble and their effects on signal transduction.Emerging evidence about possible ways of regulation of activity of these scaffolding proteins is also discussed.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Pharmacology, College of Medicine, University of Illinois at Chicago, 909 S, Wolcott Ave, Chicago, Illinois 60612, USA. tvy@uic.edu.

ABSTRACT
Heterotrimeric G proteins are ubiquitous signaling partners of seven transmembrane-domain G-protein-coupled receptors (GPCRs), the largest (and most important pharmacologically) receptor family in mammals. A number of scaffolding proteins have been identified that regulate various facets of GPCR signaling. In this review, we summarize current knowledge concerning those scaffolding proteins that are known to directly bind heterotrimeric G proteins, and discuss the composition of the protein complexes they assemble and their effects on signal transduction. Emerging evidence about possible ways of regulation of activity of these scaffolding proteins is also discussed.

No MeSH data available.


Signaling from the Gα13-radixin complex.
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Figure 3: Signaling from the Gα13-radixin complex.

Mentions: Radixin was found to interact with activated (but not GDP-bound) Gα13 via its N-terminal domain [61]. This interaction apparently disrupted the interaction between the N- and C-terminal domains, leading to radixin "conformational activation" and increased binding to F-actin [61]. Dominant-negative deletion mutants of radixin could block transformation induced by mutationally activated Gα13, suggesting that radixin could act downstream of Gα13 in this process [61]. A suggestion that radixin may mediate cellular effects of Gα13 was further substantiated by a more recent study from our laboratory, which found that the C-terminal domain of radixin activates Rac1 and CAMKII, leading to stimulation of SRE (serum response element)-dependent gene transcription ([62]; Fig. 3).


Scaffolding proteins in G-protein signaling.

Andreeva AV, Kutuzov MA, Voyno-Yasenetskaya TA - J Mol Signal (2007)

Signaling from the Gα13-radixin complex.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2211295&req=5

Figure 3: Signaling from the Gα13-radixin complex.
Mentions: Radixin was found to interact with activated (but not GDP-bound) Gα13 via its N-terminal domain [61]. This interaction apparently disrupted the interaction between the N- and C-terminal domains, leading to radixin "conformational activation" and increased binding to F-actin [61]. Dominant-negative deletion mutants of radixin could block transformation induced by mutationally activated Gα13, suggesting that radixin could act downstream of Gα13 in this process [61]. A suggestion that radixin may mediate cellular effects of Gα13 was further substantiated by a more recent study from our laboratory, which found that the C-terminal domain of radixin activates Rac1 and CAMKII, leading to stimulation of SRE (serum response element)-dependent gene transcription ([62]; Fig. 3).

Bottom Line: A number of scaffolding proteins have been identified that regulate various facets of GPCR signaling.In this review, we summarize current knowledge concerning those scaffolding proteins that are known to directly bind heterotrimeric G proteins, and discuss the composition of the protein complexes they assemble and their effects on signal transduction.Emerging evidence about possible ways of regulation of activity of these scaffolding proteins is also discussed.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Pharmacology, College of Medicine, University of Illinois at Chicago, 909 S, Wolcott Ave, Chicago, Illinois 60612, USA. tvy@uic.edu.

ABSTRACT
Heterotrimeric G proteins are ubiquitous signaling partners of seven transmembrane-domain G-protein-coupled receptors (GPCRs), the largest (and most important pharmacologically) receptor family in mammals. A number of scaffolding proteins have been identified that regulate various facets of GPCR signaling. In this review, we summarize current knowledge concerning those scaffolding proteins that are known to directly bind heterotrimeric G proteins, and discuss the composition of the protein complexes they assemble and their effects on signal transduction. Emerging evidence about possible ways of regulation of activity of these scaffolding proteins is also discussed.

No MeSH data available.