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Review
. 2005 Mar;4(3):495-503.
doi: 10.1128/EC.4.3.495-503.2005.

Except in every detail: comparing and contrasting G-protein signaling in Saccharomyces cerevisiae and Schizosaccharomyces pombe

Charles S Hoffman  1
Affiliations
Review

Except in every detail: comparing and contrasting G-protein signaling in Saccharomyces cerevisiae and Schizosaccharomyces pombe

Charles S Hoffman. Eukaryot Cell. 2005 Mar.
No abstract available

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Figures

FIG. 1.
FIG. 1.
The G-protein activation-inactivation cycle. (A) In the absence of an extracellular ligand, the G protein is present as an inactive heterotrimer (Gα is in green, Gβ is in blue, and Gγ is in red), with the Gα subunit bound to GDP. The G protein may also be bound to its cognate GPCR in a preactivation complex. Downstream effectors “A” and “B” are shown as physically separate from the G protein, although the receptor-G-protein-effector model (15) suggests that these proteins could interact with the inactive G protein, although not in a manner that leads to effector activation. (B) Ligand binding by the receptor causes the Gα subunit to release GDP and bind the more abundant GTP nucleotide. This binding results in a conformational change in the Gα and either dissociation from the Gβγ dimer or remodeling of the interaction between these subunits. The Gβγ dimer does not undergo a conformational change. (C) Once activated, the Gα, the Gβγ dimer, or both components of the G protein can activate downstream effectors. Eventually, the Gα subunit hydrolyzes the bound GTP nucleotide to GDP. This causes the Gα subunit, and thus the G protein, to return to the inactive conformation to complete the cycle.
FIG. 2.
FIG. 2.
G-protein-mediated signaling pathways of S. cerevisiae and S. pombe. Schematics identify the key receptors, G-protein subunits, and effectors, as well as some additional relevant proteins for (A) the S. cerevisiae pheromone pathway, (B) the S. pombe pheromone pathway, (C) the S. cerevisiae glucose/cAMP pathway (note that the Gpb1/2-Gpg1 Gβγ mimic may not be associated with the membrane due to the absence of a CAAX box on Gpg1), and (D) the S. pombe glucose/cAMP pathway (note the lack of an N-terminal coiled-coil domain in the Git5 Gβ). Details for each pathway are provided in the text.
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References

    1. Alspaugh, J. A., J. R. Perfect, and J. Heitman. 1997. Cryptococcus neoformans mating and virulence are regulated by the G-protein α subunit GPA1 and cAMP. Genes Dev. 11:3206-3217. - PMC - PubMed
    1. Alspaugh, J. A., R. Pukkila-Worley, T. Harashima, L. M. Cavallo, D. Funnell, G. M. Cox, J. R. Perfect, J. W. Kronstad, and J. Heitman. 2002. Adenylyl cyclase functions downstream of the Gα protein Gpa1 and controls mating and pathogenicity of Cryptococcus neoformans. Eukaryot. Cell 1:75-84. - PMC - PubMed
    1. Ansari, K., S. Martin, M. Farkasovsky, I. M. Ehbrecht, and H. Kuntzel. 1999. Phospholipase C binds to the receptor-like GPR1 protein and controls pseudohyphal differentiation in Saccharomyces cerevisiae. J. Biol. Chem. 274:30052-30058. - PubMed
    1. Bailey, W. J., W. B. Vanti, S. R. George, R. Blevins, S. Swaminathan, J. A. Bonini, K. E. Smith, R. L. Weinshank, and B. F. O'Dowd. 2001. Patent status of the therapeutically important G-protein-coupled receptors. Exp. Opin. Ther. Patents 11:1861-1887.
    1. Bar, E. E., A. T. Ellicott, and D. E. Stone. 2003. Gβγ recruits Rho1 to the site of polarized growth during mating in budding yeast. J. Biol. Chem. 278:21798-21804. - PubMed

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