Mitogen-activated protein kinase signaling in plant pathogenic fungi
The formation of Mst7 homodimers involves the thioredoxins and is important for Pmk1 activation [6]. Besides its intramolecular self-inhibitory binding, Mst11 also interacts with Ras proteins via the Ras-association domain for Pmk1 activation [7,8]. The Cochliobolus sativus Cshog1 mutant is normal i...
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Published in: | PLoS pathogens Vol. 14; no. 3; p. e1006875 |
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Main Authors: | , , , |
Format: | Journal Article |
Language: | English |
Published: |
United States
Public Library of Science
01-03-2018
Public Library of Science (PLoS) |
Subjects: | |
Online Access: | Get full text |
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Summary: | The formation of Mst7 homodimers involves the thioredoxins and is important for Pmk1 activation [6]. Besides its intramolecular self-inhibitory binding, Mst11 also interacts with Ras proteins via the Ras-association domain for Pmk1 activation [7,8]. The Cochliobolus sativus Cshog1 mutant is normal in root infection but significantly reduced in virulence on barley leaves [15]. [...]the function of this MAPK pathway in pathogenesis may be not only species-specific but also tissue-specific. Besides its conserved role in osmoregulation, this pathway has species-specific functions in pathogenesis, vegetative growth, fungicide sensitivity, sexual and asexual development, and responses to oxidative, cell wall, and other stresses in different plant pathogenic fungi. Deletion of MST50 also affects Osm1 activation in response to hyperosmotic stress, and Hik1 interacts with Mst50 [26]. Because the cyclic adenosine monophosphate-protein kinase A (cAMP-PKA) pathway also regulates various developmental and infection processes, cross-talking between cyclic adenosine monophosphate (cAMP) signaling and MAPK cascades must occur and likely involve different mechanisms in plant pathogenic fungi [1,2,27]. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 The authors have declared that no competing interests exist. |
ISSN: | 1553-7374 1553-7366 1553-7374 |
DOI: | 10.1371/journal.ppat.1006875 |