Morphogenesis of a human fungal pathogen requires septin phosphorylation.
In this issue of Developmental Cell, Sinha et al. describe a posttranscriptional mechanism necessary for hyphal development of the human pathogen, Candida albicans. In this context, the kinase Gin4 phosphorylates the septin Cdc11 in uninduced yeast cells to prime them for fast action by the cyclin-dependent kinase Cdc28/Ccn1 at the time of hyphal induction. Joint phosphorylation of Cdc11 by these two kinases is essential for stable polarization of hyphal growth.
Sudbery
Peter
P
Department of Molecular Biology and Biotechnology, Sheffield University, Western Bank, Sheffield S10 2TN, United Kingdom. p.sudbery@shef.ac.uk
D002176:Candida albicans / Q000166:cytology / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism* / Q000472:pathogenicity*; D018797:Cell Cycle Proteins / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D006801:Humans; D009024:Morphogenesis; D010766:Phosphorylation
D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins