scholarly journals Crk1, a Novel Cdc2-Related Protein Kinase, Is Required for Hyphal Development and Virulence in Candida albicans

2000 ◽  
Vol 20 (23) ◽  
pp. 8696-8708 ◽  
Author(s):  
Jiangye Chen ◽  
Song Zhou ◽  
Qin Wang ◽  
Xi Chen ◽  
Ting Pan ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Oligonucleotide Probe ◽  
Ectopic Expression ◽  
Kinase Domain ◽  
Invasive Growth ◽  
Related Protein ◽  
Cdc2 Kinase ◽  
Cyclin Dependent Kinases ◽  
Hyphal Development ◽  
Mitogen Activated Protein

ABSTRACT Both mitogen-activated protein kinases and cyclin-dependent kinases play a role in hyphal development in Candida albicans. Using an oligonucleotide probe-based screen, we have isolated a new member of the Cdc2 kinase subfamily, designated Crk1 (Cdc2-related kinase). The protein sequence of Crk1 is most similar to those ofSaccharomyces cerevisiae Sgv1 and human Pkl1/Cdk9. InS. cerevisiae, CRK1 suppresses some, but not all, of the defects associated with an sgv1 mutant. Deleting both copies of CRK1 in C. albicansslows growth slightly but leads to a profound defect in hyphal development under all conditions examined. crk1/crk1mutants are impaired in the induction of hypha-specific genes and are avirulent in mice. Consistent with this, ectopic expression of the Crk1 kinase domain (CRK1N) promotes filamentous or invasive growth in S. cerevisiae and hyphal development in C. albicans. The activity of Crk1 inS. cerevisiae requires Flo8 but is independent of Ste12 and Phd1. Similarly, Crk1 promotes filamentation through a route independent of Cph1 and Efg1 in C. albicans. RAS1V13 can also activate filamentation in acph1/cph1 efg1/efg1 double mutant. Interestingly,CRK1N produces florid hyphae in ras1/ras1strains, while RAS1V13 generates feeble hyphae in crk1/crk1 strains.

scholarly journals Corrigendum to

2021 ◽  
Author(s):  
Shuangyan Yao ◽  
Yuting Feng ◽  
Amjad Islam ◽  
Manjari Shrivastava ◽  
Hongcheng Gu ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Invasive Growth ◽  
Related Protein

scholarly journals Cyclin-Dependent Kinases Control Septin Phosphorylation in Candida albicans Hyphal Development

2007 ◽  
Vol 13 (3) ◽  
pp. 421-432 ◽  
Author(s):  
Indrajit Sinha ◽  
Yan-Ming Wang ◽  
Robin Philp ◽  
Chang-Run Li ◽  
Wai Ho Yap ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Cyclin Dependent Kinases ◽  
Hyphal Development

scholarly journals Characterization of a Candida albicans Mutant Defective in All MAPKs Highlights the Major Role of Hog1 in the MAPK Signaling Network

2020 ◽  
Vol 6 (4) ◽  
pp. 230
Author(s):  
Inês Correia ◽  
Duncan Wilson ◽  
Bernhard Hube ◽  
Jesús Pla
Keyword(s):  
Candida Albicans ◽  
Ectopic Expression ◽  
Mapk Signaling ◽  
Specific Pattern ◽  
Phenotypic Switching ◽  
Cellular Functions ◽  
Highly Sensitive ◽  
Mitogen Activated Protein ◽  
Quadruple Mutant

The success of Candida albicans as a pathogen relies on its ability to adapt and proliferate in different environmental niches. Pathways regulated by mitogen-activated protein kinases (MAPKs) are involved in sensing environmental conditions and developing an accurate adaptive response. Given the frequent cooperative roles of these routes in cellular functions, we have generated mutants defective in all combinations of the four described MAPKs in C. albicans and characterized its phenotype regarding sensitiveness to specific drugs, morphogenesis and interaction with host immune cells. We demonstrate that all MAPKs are dispensable in this yeast as a mutant defective in Cek1, Cek2, Mkc1 and Hog1 is viable although highly sensitive to oxidative and osmotic stress, displaying a specific pattern of sensitivity to antifungals. By comparing its phenotype with single, double and triple combinations of MAPK-deletion mutants we were able to unveil a Cek1-independent mechanism for Hog1 resistance to Congo red, and confirm the predominant effect of Hog1 on oxidative and osmotic adaptation. The quadruple mutant produces filaments under non-inducing conditions, but is unable to develop chlamydospores. Furthermore, cek1 cek2 mkc1 hog1 cells switch to the opaque state at high frequency, which is blocked by the ectopic expression of HOG1 suggesting a role of this kinase for phenotypic switching.

scholarly journals Loss of Arp1, a putative actin-related protein, triggers filamentous and invasive growth and impairs pathogenicity in Candida albicans

2020 ◽  
Vol 18 ◽  
pp. 4002-4015
Author(s):  
Shuangyan Yao ◽  
Yuting Feng ◽  
Amjad Islam ◽  
Manjari Shrivastava ◽  
Hongcheng Gu ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Invasive Growth ◽  
Related Protein

scholarly journals Dominant Mutations of Drosophila MAP Kinase Kinase and Their Activities in Drosophila and Yeast MAP Kinase Cascades

Genetics ◽  
1997 ◽  
Vol 146 (1) ◽  
pp. 263-273 ◽  
Author(s):  
Young-Mi Lim ◽  
Leo Tsuda ◽  
Yoshihiro H Inoue ◽  
Kenji Irie ◽  
Takashi Adachi-Yamada ◽  
...  
Keyword(s):  
Map Kinase ◽  
Tyrosine Kinases ◽  
Egf Receptor ◽  
Kinase Domain ◽  
Nucleotide Sequencing ◽  
Gain Of Function ◽  
Highly Sensitive ◽  
Mitogen Activated Protein ◽  
Signal Specificity ◽  
Map Kinase Kinase

Eight alleles of Dsor1 encoding a Drosophila homologue of mitogen-activated protein (MAP) kinase kinase were obtained as dominant suppressors of the MAP kinase kinase kinase D-raf. These Dsor1 alleles themselves showed no obvious phenotypic consequences nor any effect on the viability of the flies, although they were highly sensitive to upstream signals and strongly interacted with gain-of-function mutations of upstream factors. They suppressed mutations for receptor tyrosine kinases (RTKs); torso (tor), sevenless (sev) and to a lesser extent Drosophila EGF receptor (DER). Furthermore, the Dsor1 alleles showed no significant interaction with gain-of-function mutations of DER. The observed difference in activity of the Dsor1 alleles among the RTK pathways suggests Dsor1 is one of the components of the pathway that regulates signal specificity. Expression of Dsor1 in budding yeast demonstrated that Dsor1 can activate yeast MAP kinase homologues if a proper activator of Dsor1 is coexpressed. Nucleotide sequencing of the Dsor1 mutant genes revealed that most of the mutations are associated with amino acid changes at highly conserved residues in the kinase domain. The results suggest that they function as suppressors due to increased reactivity to upstream factors.

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