Functional interaction between the PKC1 pathway and CDC31 network of SPB duplication genes.
The earliest known step in yeast spindle pole body (SPB) duplication requires Cdc31p and Kar1p, two physically interacting SPB components, and Dsk2p and Rad23p, a pair of ubiquitin-like proteins. Components of the PKC1 pathway were found to interact with these SPB duplication genes in two independent genetic screens. Initially, SLG1 and PKC1 were obtained as high-copy suppressors of dsk2Delta rad23Delta and a mutation in MPK1 was synthetically lethal with kar1-Delta17. Subsequently, we demonstrated extensive genetic interactions between the PKC1 pathway and the SPB duplication mutants that affect Cdc31p function. The genetic interactions are unlikely to be related to the cell-wall integrity function of the PKC1 pathway because the SPB mutants did not exhibit cell-wall defects. Overexpression of multiple PKC1 pathway components suppressed the G2/M arrest of the SPB duplication mutants and mutations in MPK1 exacerbated the cell cycle arrest of kar1-Delta17, suggesting a role for the PKC1 pathway in SPB duplication. We also found that mutations in SPC110, which encodes a major SPB component, showed genetic interactions with both CDC31 and the PKC1 pathway. In support of the model that the PKC1 pathway regulates SPB duplication, one of the phosphorylated forms of Spc110p was absent in pkc1 and mpk1Delta mutants.
Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544-1014, USA.
W
W
Khalfan
I
I
Ivanovska
M D
MD
Rose
D015153:Blotting, Western; D002135:Calcium-Binding Proteins / Q000235:genetics*; D002148:Calmodulin-Binding Proteins; D018797:Cell Cycle Proteins / Q000235:genetics*; D003598:Cytoskeletal Proteins; D004268:DNA-Binding Proteins / Q000235:genetics; D005656:Fungal Proteins / Q000235:genetics* / Q000378:metabolism; D016195:G2 Phase; D015966:Gene Expression Regulation, Fungal; D005816:Genetic Complementation Test; D008565:Membrane Proteins / Q000235:genetics; D020928:Mitogen-Activated Protein Kinases; D008938:Mitosis; D009154:Mutation; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism; D010641:Phenotype; D010766:Phosphorylation; D011493:Protein Kinase C; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins; D008941:Spindle Apparatus / Q000235:genetics*; D013696:Temperature; D013997:Time Factors; D014452:Ubiquitins / Q000235:genetics
C083769:CDC31 protein, S cerevisiae; D002135:Calcium-Binding Proteins; D002148:Calmodulin-Binding Proteins; D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D004268:DNA-Binding Proteins; C100415:DSK2 protein, S cerevisiae; D005656:Fungal Proteins; C074559:KAR1 protein, S cerevisiae; D008565:Membrane Proteins; D009687:Nuclear Proteins; C490846:RAD23 protein, S cerevisiae; C119383:SLG1 protein, S cerevisiae; C073277:SPC110 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014452:Ubiquitins; C097993:Pkc1 protein, Trichoderma reesei; D011493:Protein Kinase C; D020928:Mitogen-Activated Protein Kinases; C072724:SLT2 protein, S cerevisiae