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Phosphorylation of Bni4 by MAP kinases contributes to septum assembly during yeast cytokinesis

AuthorsPérez, Jacqueline ; Arcones, Irene ; Gómez, Alberto ; Casquero, Verónica ; Roncero, Cesar
Septum assembly
MAP kinase
Issue Date2016
PublisherOxford University Press
CitationFEMS Yeast Research 16(6): fow060 (2016)
AbstractPrevious work has shown that the synthetic lethality of the slt2Δrim101Δ mutant results from a combination of factors, including improper functioning of the septum assembly machinery. Here, we identify new multicopy suppressors of this lethality including Kss1, Pcl1 and Sph1, none of which seems to be linked to the upregulation of chitin synthesis. Characterization of the suppression mediated by Kss1 showed that it is independent of the transcriptional response of the CWI signaling response, but efficiently restores the Bni4 localization defects produced by the absence of Slt2. Accordingly, Bni4 interacts physically with both kinases, and its levels of phosphorylation are reduced in the slt2Δ mutant but increased after Kss1 overexpression. Using an assay based on hypersensitive cells of the cdc10-11 mutant, we have pinpointed several MAP kinase phosphorylatable residues required for Bni4 function. Our results, together with a genetic correlation analysis, strongly support a functional model linking Slt2 MAP kinase and Pcl1, a Pho85 cyclin-dependent kinase, in septum assembly through Bni4. This model, based on the coordinated phosphorylation of Bni4 by both kinases, would be able to integrate cellular signals rapidly to maintain cell integrity during cytokinesis.
Publisher version (URL)https://doi.org/10.1093/femsyr/fow060
Identifiersdoi: 10.1093/femsyr/fow060
e-issn: 1567-1364
issn: 1567-1356
Appears in Collections:(IBFG) Artículos
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