14-3-3
proteins are found in all eukaryotes where they function as regulators
of a wide range of biological processes. They function by interacting directly
with numerous different target proteins thereby altering their activity.
Interactions are generally mediated by phosphorylation of specific binding
sites in the target proteins. 14-3-3 binding can either:
-
directly
alter protein activity (either positively or negatively),
-
control
nuclear-cytoplasmic shuttling,
-
mediate
protein import into mitochondria and chloroplasts,
-
form a
scaffold to permit interactions between two different binding proteins.
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We
are particularly interested in identifying and characterising roles for
14-3-3s in plant cell signalling.
Plant
defence responses to pathogens are a major focus for us, and we have identified
calmodulin-domain protein kinases (CDPK), MAP kinase pathways, lipoxygenases
and ion channels as potential
targets for 14-3-3 proteins important in defence. We use the tomato
Cf9/Avr9 resistance response as a model, and have identified 12 different
14-3-3
genes in tomato, three of which are pathogen responsive. |
As
well as taking molecular genetic and biochemical approaches to investigate
14-3-3 protein-protein interactions in plant defence responses, we are
also interested to determine whether and how different 14-3-3 isoforms
play specific roles in the plant. This will be achieved through:
-
kinetic
analysis of 14-3-3 protein-protein interactions,
-
structural
analysis of plant 14-3-3 protein complexes,
-
detailed
analysis of the regulation of expression and localisation of plant 14-3-3
proteins.
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