title: Extracellular invertase: key metabolic enzyme and PR protein.
abstract: Extracellular invertase is the key enzyme of an apoplasmic phloem unloading pathway and catalyses the hydrolytic cleavage of the transport sugar sucrose released into the apoplast. This mechanism contributes to long-distance assimilate transport, provides the substrate to sustain heterotrophic growth and generates metabolic signals known to effect various processes of primary metabolism and defence responses. The essential function of extracellular invertase for supplying carbohydrates to sink organs was demonstrated by the finding that antisense repression of an anther-specific isoenzyme provides an efficient method for metabolic engineering of male sterility. The regulation of extracellular invertase by all classes of phytohormones indicates an essential link between the molecular mechanism of phytohormone action and primary metabolism. The up-regulation of extracellular invertase appears to be a common response to various biotic and abiotic stress-related stimuli such as pathogen infection and salt stress, in addition to specific stress-related reactions. Based on the observed co-ordinated regulation of source/sink relations and defence responses by sugars and stress-related stimuli, the identified activation of distinct subsets of MAP kinases provides a mechanism for signal integration and distribution within such complex networks. Sucrose derivatives not synthesized by higher plants, such as turanose, were shown to elicit responses distinctly different from metabolizable sugars and are rather perceived as stress-related stimuli.
authors.affiliation: Lehrstuhl für Pharmazeutische Biologie, Julius-von-Sachs Institute, Julius-von-Sachs-Platz 2, Universität Würzburg, D-97082 Würzburg, Germany. Roitsch@biozentrum.uni-wuerzburg.de
authors.forename: T
authors.initials: T
authors.lastname: Roitsch
authors.forename: M E
authors.initials: ME
authors.lastname: Balibrea
authors.forename: M
authors.initials: M
authors.lastname: Hofmann
authors.forename: R
authors.initials: R
authors.lastname: Proels
authors.forename: A K
authors.initials: AK
authors.lastname: Sinha
mesh_terms: D004190:Disasters; D005110:Extracellular Space / Q000201:enzymology; D005298:Fertility / Q000235:genetics / Q000502:physiology; D035264:Flowers / Q000235:genetics / Q000378:metabolism; D015971:Gene Expression Regulation, Enzymologic / Q000187:drug effects; D018506:Gene Expression Regulation, Plant / Q000187:drug effects; D006026:Glycoside Hydrolases / Q000235:genetics / Q000378:metabolism*; D007113:Immunity, Innate / Q000235:genetics; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism; D010935:Plant Diseases / Q000382:microbiology; D010937:Plant Growth Regulators / Q000494:pharmacology; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D010944:Plants / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics; D015398:Signal Transduction / Q000235:genetics / Q000502:physiology; D012965:Sodium Chloride / Q000494:pharmacology; D013379:Substrate Specificity; D013696:Temperature; D014867:Water / Q000502:physiology; D043324:beta-Fructofuranosidase
chemical_list: D007527:Isoenzymes; D010937:Plant Growth Regulators; D010940:Plant Proteins; C053376:pathogenesis-related proteins, plant; D014867:Water; D012965:Sodium Chloride; D020928:Mitogen-Activated Protein Kinases; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase