This effect too is specific to CaRas1 and ScRas2 is unable to replicate it. This has direct consequences for expression of CaERG11, encoding the target of azole antifungals. In turn, CaGPI2 downregulates CaGPI19, encoding another GPI-GnT subunit. Interestingly, CaRas1 transcriptionally activates CaGPI2, encoding a GPI-GnT subunit that has been shown to interact with CaRas1 physically. That CaRas1 alone activates GPI-GnT and not ScRas2 suggests that this process is cAMP independent. However, ScRas2 is unable to activate the GPI- N -acetylglucosaminyl transferase (GPI-GnT) which catalyzes the first step of GPI biosynthesis. We show that ScRas2 functionally complements CaRas1 in rescuing growth as well as activating hyphal growth, a process that involves plasma membrane localized Ras activating cAMP/PKA signaling via Cyr1. In order to understand how extensive is the functional homology between the highly homologous proteins, S. cerevisiae Ras2 and C. albicans Ras1, we examined whether ScRas2 could functionally complement CaRas1 in activating hyphal morphogenesis as well as GPI anchor biosynthesis. GTP-bound Ras binds to effectors to trigger signaling cascades. Ras proteins are highly conserved small GTPases in eukaryotes.
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