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• W2122886976 abstract "Recent evidence indicates that several mechanisms can alter invertase activity and, thus, affect sucrose metabolism and resource allocation in plants. One of these mechanisms is the compartmentalisation of at least some vacuolar invertases in precursor protease vesicles (PPV), where their retention could control timing of delivery to vacuoles and hence activity. PPV are small, ER-derived bodies that sequester a subset of vacuolar-bound proteins (such as invertases and protease precursors) releasing them to acid vacuoles in response to developmental or environmental signals. Another newly-identified effector of invertases is wall-associated kinase 2 (WAK2), which can regulate a specific vacuolar invertase in Arabidopsis (AtvacINV1) and alter root growth when osmolyte supplies are limiting. WAKs are ideally positioned to sense changes in the interface between the cell wall and plasma membrane (such as turgor), because the N-terminus of each WAK extends into the cell wall matrix (where a pectin association is hypothesised) and the C-terminus has a cytoplasmic serine/threonine kinase domain (signalling). Still other avenues of invertase control are provided by a diverse group of kinases and phosphatases, consistent with input from multiple sensing systems for sugars, pathogens, ABA and other hormones. Mechanisms of regulation may also vary for the contrasting sugar responses of different acid invertase transcripts. Some degree of hexokinase involvement and distinctive kinetics have been observed for the sugar-repressed invertases, but not for the more common, sugar-induced forms examined thus far. An additional means of regulation for invertase gene expression lies in the multiple DST (Down STream) elements of the 3′ untranslated region for the most rapidly repressed invertases. Similar sequences were initially identified in small auxin-up RNAs (SAUR) where they mediate rapid mRNA turnover. Finally, the invertase inhibitors, cell wall- and vacuolar inhibitors of fructosidase (CIF and VIF, respectively) are indistinguishable by sequence alone from pectin methylesterase inhibitors (PMEI); however, recent evidence suggests binding specificity may be determined by flexibility of a short, N-terminal region. These recently characterised processes increase the suite of regulatory mechanisms by which invertase – and, thus, sucrose metabolism and resource partitioning – can be altered in plants." @default.
• W2122886976 created "2016-06-24" @default.
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• W2122886976 date "2007-01-01" @default.
• W2122886976 modified "2023-10-18" @default.
• W2122886976 title "Regulation of invertase: a 'suite' of transcriptional and post-transcriptional mechanisms" @default.
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• W2122886976 doi "https://doi.org/10.1071/fp06227" @default.
• W2122886976 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32689379" @default.
• W2122886976 hasPublicationYear "2007" @default.
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