The fusicoccin story revisited
Abstract Fusicoccin (FC) is one of the most studied fungal metabolites to date. The finding that the plasma membrane H+-ATPase in combination with 14-3-3 proteins acts as a high-affinity receptor for FC was a breakthrough in the field. Ever since, the binding of FC to the ATPase–14-3-3 receptor comp...
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Published in | Journal of experimental botany Vol. 75; no. 18; pp. 5531 - 5546 |
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Main Author | |
Format | Journal Article |
Language | English |
Published |
UK
Oxford University Press
27.09.2024
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Subjects | |
Online Access | Get full text |
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Summary: | Abstract
Fusicoccin (FC) is one of the most studied fungal metabolites to date. The finding that the plasma membrane H+-ATPase in combination with 14-3-3 proteins acts as a high-affinity receptor for FC was a breakthrough in the field. Ever since, the binding of FC to the ATPase–14-3-3 receptor complex has taken center stage in explaining all FC-induced physiological effects. However, a more critical review shows that this is not evident for a number of FC-induced effects. This review challenges the notion that all FC-affected processes start with the binding to and activation of the plasma membrane ATPase, and raises the question of whether other proteins with a key role in the respective processes are directly targeted by FC. A second unresolved question is whether FC may be another example of a fungal molecule turning out to be a ‘copy’ of an as yet unknown plant molecule. In view of the evidence, albeit not conclusive, that plants indeed produce ‘FC-like ligands’, it is worthwhile making a renewed attempt with modern improved technology to answer this question; the answer might upgrade FC or its structural analogue(s) to the classification of plant hormone.
In this review, two questions are addressed: are all effects that fusicoccin has on the physiology of plants the result of H+ -ATPase activation; and do plants produce fusicoccin(-like) molecules? |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 |
ISSN: | 0022-0957 1460-2431 1460-2431 |
DOI: | 10.1093/jxb/erae300 |