The phosphatidylinositol 3-kinase Vps34p of the human pathogenic yeast Candida albicans is a multifunctional protein that interacts with the putative vacuolar H +-ATPase subunit Vma7p

The phosphatidylinositol 3-kinase Vps34p of Candida albicans participates in protein transport and in virulence. In order to characterize the functional link between these two activities we searched for proteins interacting with C. albicans Vps34p and demonstrate physical interaction of Vps34p with...

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Bibliographic Details
Published in:International journal of medical microbiology 2005-04, Vol.295 (1), p.57-66
Main Authors: Eck, Raimund, Nguyen, Monika, Günther, Juliane, Künkel, Waldemar, Zipfel, Peter F.
Format: Article
Language:English
Subjects:
Autophagy - physiology
Candida albicans
Candida albicans - enzymology
Candida albicans - metabolism
Gene Deletion
Genes, Fungal
Hydrogen-Ion Concentration
Phosphatidylinositol 3-Kinases - genetics
Phosphatidylinositol 3-Kinases - metabolism
Protein Binding
Protein Interaction Mapping
PtdIns 3-kinase
Two-Hybrid System Techniques
V-ATPase
Vacuolar Proton-Translocating ATPases - metabolism
Vacuoles - metabolism
Virulence
Vma7p
Vps34p
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Summary:The phosphatidylinositol 3-kinase Vps34p of Candida albicans participates in protein transport and in virulence. In order to characterize the functional link between these two activities we searched for proteins interacting with C. albicans Vps34p and demonstrate physical interaction of Vps34p with the subunit of the vacuolar H +-ATPase Vma7p. The interaction initially observed in a yeast two-hybrid system was confirmed in vitro with recombinant proteins. Functional assays show that the Vps34p protein is necessary for vacuolar acidification and growth at alkaline pH. In addition, the vps34 null mutant of C. albicans shows defective autophagocytosis. The relevance of these functions for virulence of C. albicans is discussed.
ISSN:1438-4221
1618-0607
DOI:10.1016/j.ijmm.2004.12.007