Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 148-160 |
| Number of pages | 13 |
| Journal | FEBS Letters |
| Volume | 590 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2016 Jan 1 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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Direct interaction of Ste11 and Mkk1/2 through Nst1 integrates high-osmolarity glycerol and pheromone pathways to the cell wall integrity MAPK pathway. / Leng, Gang; Song, Kiwon.
In: FEBS Letters, Vol. 590, No. 1, 01.01.2016, p. 148-160.Research output: Contribution to journal › Article
TY - JOUR
T1 - Direct interaction of Ste11 and Mkk1/2 through Nst1 integrates high-osmolarity glycerol and pheromone pathways to the cell wall integrity MAPK pathway
AU - Leng, Gang
AU - Song, Kiwon
PY - 2016/1/1
Y1 - 2016/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84956607631&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84956607631&partnerID=8YFLogxK
U2 - 10.1002/1873-3468.12039
DO - 10.1002/1873-3468.12039
M3 - Article
C2 - 26787465
AN - SCOPUS:84956607631
VL - 590
SP - 148
EP - 160
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1
ER -