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Protein kinase C participates in a cell growth network in the filamentous fungus Aspergillus nidulans

The long‐term goal of our research is to advance understanding of the mechanisms involved in hyphal growth and the synthesis and maintenance of cell walls in filamentous fungi. Recently our work has focused on proteins that localize to sites of cell wall synthesis, namely growing cell apices (hyphal tips) and forming crosswalls (septa). PkcA, an orthologue of protein kinase C in our model organism Aspergillus nidulans, is one such protein. In previous work, we identified a mutation in the pkcA gene which results in reduced cell wall integrity. We showed that wild type PkcA localizes to growing hyphal apices and septation sites, and we identified amino acid sequences within PkcA that are required in order for PkcA to localize to these sites of cell wall synthesis. Our work, as well as work done in other labs, has also brought to light many other proteins that play roles in septation and polarized growth and that also localize to septation sites and growing tips. Here we report our work towards placing PkcA and other polarized growth related proteins in a cell growth network. Using a collection of mutant strains carrying dual labels (GFP and monomeric RFP) of PkcA and other polarized growth related proteins, we showed via fluorescence microscopy that PkcA colocalizes with the actinin‐like protein AcnA, the septin AspB, BimG phosphatase, landmark protein Bud4, Cdc14 phosphatase, septation initiation complex component MobA, Rho4 GTPase, myosin regulatory light chain (Rlc1), the formin SepA, and the IQGAP homologue SepG at hyphal tips and/or septation sites. We also observed PkcA localization in a variety of strains in which expression of other growth related proteins had been genetically disrupted. In addition, the current results have begun establishing which proteins PkcA physically binds at tips and septation sites. Using bimolecular fluorescence complementation we demonstrated that PkcA and SepA might physically interact at both tips and septation sites. Our future work will include investigating other physical interactions with PkcA and determining which complexed proteins are solely involved in localization and regulation and which are PkcA substrates.