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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.


Scaffolding proteins that link subunits of heterotrimeric G proteins with MAP kinase cascade. A, The role of Ste5 in the mating signaling in yeast. B, Signaling complex assembled by KSR1, leading to ERK activation. C, Signaling complex assembled by JLP, leading to activation of JNK (or p38, see discussion in the main text). LPA, lysophosphatidic acid; RA, retinoic acid.
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Figure 5: Scaffolding proteins that link subunits of heterotrimeric G proteins with MAP kinase cascade. A, The role of Ste5 in the mating signaling in yeast. B, Signaling complex assembled by KSR1, leading to ERK activation. C, Signaling complex assembled by JLP, leading to activation of JNK (or p38, see discussion in the main text). LPA, lysophosphatidic acid; RA, retinoic acid.

Mentions: Scaffolding proteins that link heterotrimeric G proteins with MAP kinase cascades. The first such scaffolding protein, Ste5, was discovered in yeast (reviewed by [72,73]). Ste5 is able to bind all three kinases (MAPKKK, MAPKK and MAPK) of the mating pathway, which promotes their mutual interactions and thereby facilitates signal transmission. Ste5 also binds to Gβγ. The latter property allows the recruitment of the Ste5/MAPK signaling complex to the stimulus-sensing receptor/G protein module, enabling signal transduction from GPCR via Gβγ to the MAPK cascade (Fig. 5A). Analogs of Ste5 act as scaffolds for other MAP kinase cascades in both yeast and mammalian cells [74,75], and some of them are also able to interact with subunits of heterotrimeric G proteins.


Scaffolding proteins in G-protein signaling.

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

Scaffolding proteins that link subunits of heterotrimeric G proteins with MAP kinase cascade. A, The role of Ste5 in the mating signaling in yeast. B, Signaling complex assembled by KSR1, leading to ERK activation. C, Signaling complex assembled by JLP, leading to activation of JNK (or p38, see discussion in the main text). LPA, lysophosphatidic acid; RA, retinoic acid.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 5: Scaffolding proteins that link subunits of heterotrimeric G proteins with MAP kinase cascade. A, The role of Ste5 in the mating signaling in yeast. B, Signaling complex assembled by KSR1, leading to ERK activation. C, Signaling complex assembled by JLP, leading to activation of JNK (or p38, see discussion in the main text). LPA, lysophosphatidic acid; RA, retinoic acid.
Mentions: Scaffolding proteins that link heterotrimeric G proteins with MAP kinase cascades. The first such scaffolding protein, Ste5, was discovered in yeast (reviewed by [72,73]). Ste5 is able to bind all three kinases (MAPKKK, MAPKK and MAPK) of the mating pathway, which promotes their mutual interactions and thereby facilitates signal transmission. Ste5 also binds to Gβγ. The latter property allows the recruitment of the Ste5/MAPK signaling complex to the stimulus-sensing receptor/G protein module, enabling signal transduction from GPCR via Gβγ to the MAPK cascade (Fig. 5A). Analogs of Ste5 act as scaffolds for other MAP kinase cascades in both yeast and mammalian cells [74,75], and some of them are also able to interact with subunits of heterotrimeric G proteins.

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.