Journal
FUNGAL GENETICS AND BIOLOGY
Volume 81, Issue -, Pages 120-131Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.fgb.2015.04.007
Keywords
CpcB; G beta-like protein; GpaB; Virulence; Conidiation; Aspergillus fumigatus
Categories
Funding
- National Natural Science Foundation of China [NSFC31370112, NSFC81330035]
- Natural Science Foundation of Jiangsu Higher Education Institutions of China [11KJA180005]
- Special Fund for Doctoral Program of Higher Education of China [20123207110012]
- Priority Academic Program Development (PAPD) of Jiangsu Higher Education Institutions and the Research
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CpcB (cross pathway control B) encodes a yeast Cpc2 and mammalian RACK1 (receptor for activated protein kinase C) ortholog, which is a WD repeat protein with functional homology to the beta subunit of heterotrimeric G proteins in Aspergillus fumigatus. Previous study has reported that CpcB governs growth and development in both A. fumigatus and Aspergillus nidulans. However, little is known about the functional identities of CpcB orthologs and their relationships with G protein complexes. In this study, we verified that cytoplasmic AfCpcB acts as a G beta-like protein ortholog and plays important roles in hyphal growth, conidiophore morphology, cell wall integrity, and virulence in A. fumigatus. Furthermore, double deletion of AfcpcB and AfgpaB (G alpha) causes a similar phenotype to AfgpaB mutant with abnormal multiple septa conidiophores but exhibits sparse conidiation with white and fluffy colonies. Thus, the exacerbated conidiation defect suggests that AfcpcB has its own specific function compared to the Got subunit of AfgpaB or the G-protein complex. In addition, complementation assays using AfcpcB orthologs of A. nidulans and yeasts (Saccharomyces cerevisiae, Schizosaccharomyces pombe, Candida albicans) suggest that all tested fungal AfcpcB orthologs under the A. fumigatus native promoter can largely restore hyphal growth defects in AfcpcB deletion mutant, but only the A. nidulans cpcB ortholog completely rescues the Delta AfcpcB conidiation defect, suggesting that CpcB acts as a G beta-like protein ortholog in the Aspergilli, but may have unique and important unexplored functions that required for conidiation, which is absent in yeast. (C) 2015 Elsevier Inc. All rights reserved.
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