Gpr1p, a Putative G-Protein Coupled Receptor, Regulates Glucose-Dependent Cellular cAMP Level in YeastSaccharomyces cerevisiae

Yun, Cheol Won; Tamaki, Hiroyuki; Nakayama, Reiko; Yamamoto, Kenji; Kumagai, Hidehiko

doi:10.1006/bbrc.1998.9600

Cited by 87 publications

(84 citation statements)

References 21 publications

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“…Second, the defect in pseudohyphal growth conferred by a gpa2∆ or gpr1∆ mutation is reversed by the addition of cAMP (Kübler et al, 1997;Lorenz and Heitman, 1997;Lorenz et al, 2000;Tamaki et al, 2000). Finally, a gpa2∆ or gpr1∆ mutation eliminates the glucose-induced increase in cAMP levels under certain conditions (Colombo et al, 1998;Kraakman et al, 1999;Lorenz et al, 2000;Yun et al, 1998). Gpa2p has been shown to function independently of Ras, which would be consistent with the possibility that Gpa2p directly activates adenylyl cyclase (Colombo et al, 1998;Xue et al, 1998).…”

mentioning

confidence: 64%

Krh1p and Krh2p act downstream of the Gpa2p Gα subunit to negatively regulate haploid invasive growth

Batlle

Green

et al. 2003

Journal of Cell Science

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The yeast Gα subunit Gpa2p and its coupled receptor Gpr1p function in a signaling pathway that is required for the transition to pseudohyphal and invasive growth. A two-hybrid screen using a constitutively active allele of GPA2 identified the KRH1 gene as encoding a potential binding partner of Gpa2p. Strains containing deletions of KRH1 and its homolog KRH2 were hyper-invasive and displayed a high level of expression of FLO11, a gene involved in pseudohyphal and invasive growth. Therefore, KRH1 and KRH2 encode negative regulators of the invasive growth pathway. Cells containing krh1Δ krh2Δ mutations also displayed increased sensitivity to heat shock and decreased sporulation efficiency, indicating that Krh1p and Krh2p regulate multiple processes controlled by the cAMP/PKA pathway. The krh1Δ krh2Δ mutations suppressed the effect of a gpa2Δ mutation on FLO11 expression and eliminated the effect of a constitutively active GPA2 allele on induction of FLO11 and heat shock sensitivity, suggesting that Krh1p and Krh2p act downstream of Gpa2p. The Sch9p kinase was not required for the signal generated by deletion of KRH1 and KRH2; however, the cAMP-dependent kinase Tpk2p was required for generation of this signal. These results support a model in which activation of Gpa2p relieves the inhibition exerted by Krh1p and Krh2p on components of the cAMP/PKA signaling pathway.

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mentioning

confidence: 64%

Krh1p and Krh2p act downstream of the Gpa2p Gα subunit to negatively regulate haploid invasive growth

Batlle

Green

et al. 2003

Journal of Cell Science

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“…In the second case, glucose binds to the receptor Gpr1 (16), which activates the G␣ protein Gpa2, which in turn activates the adenylyl cyclase Cyr1 (13-27, 53, 54). Activation of Cyr1 leads to a rapid and transient increase in cellular concentrations of cAMP (19).…”

Section: Asc1 Functions As a Guanine Nucleotide Dissociationmentioning

confidence: 99%

“…All of these proteins are required for glucoseinduced cAMP signaling (13) and pseudohyphal differentiation (14,15). There is also evidence for physical association of glucose with Gpr1 (16), Gpr1 with Gpa2 (17)(18)(19), and Gpa2 with Cyr1 (20,21). The resulting increase in cAMP promotes activation of the cAMP-dependent protein kinase (22)(23)(24)(25)(26)(27).…”

mentioning

confidence: 99%

The RACK1 Ortholog Asc1 Functions as a G-protein β Subunit Coupled to Glucose Responsiveness in Yeast

Zeller

Parnell

Dohlman

2007

Journal of Biological Chemistry

130

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According to the prevailing paradigm, G-proteins are composed of three subunits, an ␣ subunit with GTPase activity and a tightly associated ␤␥ subunit complex. In the yeast Saccharomyces cerevisiae there are two known G␣ proteins (Gpa1 and Gpa2) but only one G␤␥, which binds only to Gpa1. Here we show that the yeast ortholog of RACK1 (receptor for activated protein kinase C1) Asc1 functions as the G␤ for Gpa2. As with other known G␤ proteins, Asc1 has a 7-WD domain structure, interacts directly with the G␣ in a guanine nucleotide-dependent manner, and inhibits G␣ guanine nucleotide exchange activity. In addition, Asc1 binds to the effector enzyme adenylyl cyclase (Cyr1), and diminishes the production of cAMP in response to glucose stimulation. Thus, whereas Gpa2 promotes glucose signaling through elevated production of cAMP, Asc1 has opposing effects on these same processes. Our findings reveal the existence of an unusual G␤ subunit, one having multiple functions within the cell in addition to serving as a signal transducer for cell surface receptors and intracellular effectors.

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“…In Saccharomyces cerevisiae, cAMP plays an important role in nutrient sensing. 1) In heterobasidiomycete Cryptococcus neoformans, hyphal differentiation and virulence are controlled by cAMP level. 2) In the corn smut fungus Ustilago maydis, intracellular cAMP levels are regulated for subsequent fungal development in plants.…”

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confidence: 99%

Elevation of Intracellular cAMP Levels by Dominant Active Heterotrimeric G Protein Alpha SubunitsScGP-AandScGP-Cin Homobasidiomycete,Schizophyllum commune

Yamagishi

Kimura

Suzuki

et al. 2004

Bioscience, Biotechnology, and Biochemistry

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Gpr1p, a Putative G-Protein Coupled Receptor, Regulates Glucose-Dependent Cellular cAMP Level in YeastSaccharomyces cerevisiae

Cited by 87 publications

References 21 publications

Krh1p and Krh2p act downstream of the Gpa2p Gα subunit to negatively regulate haploid invasive growth

Krh1p and Krh2p act downstream of the Gpa2p Gα subunit to negatively regulate haploid invasive growth

The RACK1 Ortholog Asc1 Functions as a G-protein β Subunit Coupled to Glucose Responsiveness in Yeast

Elevation of Intracellular cAMP Levels by Dominant Active Heterotrimeric G Protein Alpha SubunitsScGP-AandScGP-Cin Homobasidiomycete,Schizophyllum commune

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