Hsp90 Orchestrates Temperature-Dependent Candida albicans Morphogenesis via Ras1-PKA Signaling

In the citing paper

“Under these conditions, the MAL2p-HSP90/hsp90Δ strain has reduced growth rate and reaches approximately half the stationary phase cell density as a wild-type strain [40].”

In the citing paper

“Our previous work established that genetic reduction of Hsp90 levels enhances the efficacy of fluconazole in a murine model of disseminated C. albicans infection [22] and that further genetic depletion of C. albicans Hsp90 results in complete clearance of an infection in the murine model [40].”

In the citing paper

“As expected, exposure of cells containing the UTR2-lacZ reporter to calcium chloride resulted in activation of calcineurin relative to the untreated control (P<0.001, ANOVA, Bonferroni's Multiple Comparison Test Figure 4C).”

In the citing paper

“Hsp90 also modulates key virulence traits in C. albicans, such as the ability to undergo morphogenesis, and in animal models, genetic compromise of Hsp90 function leads to clearance of otherwise lethal Candida or Aspergillus infections (Cowen et al. 2009; Shapiro et al. 2009).”

In the citing paper

“Hsp90 functions as a signaling hub, stabilizing various signal transducers that modulate key fungal virulence phenotypes (Cowen and Lindquist 2005; Shapiro et al. 2009; O’Meara et al. 2019; Hossain et al. 2020).”

In the citing paper

“In C. albicans, Hsp90 modulates cellular responses to antifungals by stabilizing components of the Pkc1-MAPK and calcineurin stress-response pathways (Cowen and Lindquist 2005; Cowen et al. 2009; Shapiro et al. 2009).”

In the citing paper

“At elevated temperatures (circa 37°C) this Hsp90 repression is relieved, leading to filamentation.”

In the citing paper

“Hsp90 regulates morphogenesis in C. albicans by repressing Ras1-PKA signalling at relatively low temperatures115.”

In the citing paper

“The molecular chaperone Hsp90 regulates morphogenesis of the leading human fungal pathogen Candida albicans.”

In the citing paper

“Hsp90 is a key temperature sensor governing morphogenesis, given that reduction of Hsp90 function bypasses the requirement for elevated temperature for cues such as serum to induce filamentous growth and that Hsp90 function is partially compromised in conditions that induce hyphal morphogenesis (Shapiro et al., 2009).”

In the citing paper

“Recently the molecular chaperone heat shock protein 90 (Hsp90) has been implicated as an important regulator of the temperature-dependent switch between yeast and filamentous growth in C. albicans (Shapiro et al., 2009).”

In the citing paper

“Depletion of Hsp90 also leads to clearance of kidney fungal burden in a mouse model of candidiasis (Shapiro et al., 2009).”

In the citing paper

“Hsp90 is an important molecular chaperone that governs key virulence traits in C. albicans (Cowen and Lindquist, 2005; Shapiro et al., 2009; Singh et al., 2009).”

In the citing paper

“Hsp90 regulates temperature-dependent morphogenesis by exerting a repressive effect on Ras1-PKA signaling, which is alleviated upon temperature elevation (Shapiro et al., 2009).”

In the citing paper

“Hsp90, an essential molecular chaperone [1,3,5,6], has been shown to govern various aspects of C. albicans pathogenicity determinants including morphological yeast to hyphal transition [7], emergence of drug resistance [8–10] and biofilm formation [11].”

In the citing paper

“Interestingly Hsp90 has been shown to be the regulator of this switch by repressing the Ras1-PKA signaling pathway [7].”

In the citing paper

“In addition to its role in enabling the emergence and maintenance of azole resistance, Hsp90 governs temperature-dependent morphogenesis in C. albicans (19).”

In the citing paper

“Hsp90 represses filamentous growth in C. albicans such that compromising Hsp90 function induces the yeast-to-filament transition by relieving repression on Ras1-protein kinase A (PKA) signaling (19).”

In the citing paper

“Depletion of Hsp90 also induces filamentation by relieving Hsp90-mediated repression of the cAMP-PKA signaling pathway (181).”