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- W2074863954 endingPage "504" @default.
- W2074863954 startingPage "496" @default.
- W2074863954 abstract "Plants respond to diverse biotic and abiotic stimuli as well as to endogenous developmental cues. Many of these stimuli result in altered activity of phospholipase D (PLD), an enzyme that hydrolyzes structural phospholipids producing phosphatidic acid (PA). PA is a key signaling intermediate in animals, but its targets in plants are relatively uncharacterized. Recent studies have demonstrated that the cytoskeleton is a major target of PLD-PA signaling and identified a positive feedback loop between actin turnover and PLD activity. Moreover, two cytoskeletal proteins, capping protein and MAP65-1, have been identified as PA-binding proteins regulating actin and microtubule organization and dynamics. In this review, we highlight the role of the PLD-PA module as an important hub for housekeeping and stress-induced regulation of membrane-associated cytoskeletal dynamics." @default.
- W2074863954 created "2016-06-24" @default.
- W2074863954 creator A5019538440 @default.
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- W2074863954 creator A5074302707 @default.
- W2074863954 creator A5088741983 @default.
- W2074863954 creator A5089014804 @default.
- W2074863954 date "2013-09-01" @default.
- W2074863954 modified "2023-10-17" @default.
- W2074863954 title "Regulation of cytoskeletal dynamics by phospholipase D and phosphatidic acid" @default.
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- W2074863954 doi "https://doi.org/10.1016/j.tplants.2013.04.005" @default.
- W2074863954 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23664415" @default.
- W2074863954 hasPublicationYear "2013" @default.