Coordination and cross talks of MAPK pathways are critical for signaling efficiency, but their mechanisms are not well understood. Slt2, the MAP kinase of cell wall integrity pathway (CWI), is activated by heat stress even in the absence of upstream components of this pathway, suggesting a supplementary input for Slt2 activation. Here, we identify a new interaction of Ste11 and Mkk1, mediated by Nst1 that connects the high-osmolarity glycerol and pheromone pathways directly to CWI pathway in response to heat and pheromone. We suggest that Ser407 and Thr411 are novel residues of Mkk1 activated by these MAPK pathways.
Bibliographical noteFunding Information:
The authors appreciate Dr. Daniel J. Lew (Duke University Medical Center) for providing the DLY1, DLY3994, and DLY4351 strains and the pDLB824 plasmid. This work was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Science, ICT and Future Planning (NRF- 2014R1A1A3051707).
© 2015 Federation of European Biochemical Societies.
All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology
- Cell Biology