| Literature DB >> 30737267 |
Kjell De Vriese1,2, Ellie Himschoot1,2, Kai Dünser3, Long Nguyen4,5, Andrzej Drozdzecki4,5, Alex Costa6, Moritz K Nowack1,2, Jürgen Kleine-Vehn3, Dominique Audenaert4,5, Tom Beeckman1,2, Steffen Vanneste7,2,8.
Abstract
Many signal perception mechanisms are connected to Ca2+-based second messenger signaling to modulate specific cellular responses. The well-characterized plant hormone auxin elicits a very rapid Ca2+ signal. However, the cellular targets of auxin-induced Ca2+ are largely unknown. Here, we screened a biologically annotated chemical library for inhibitors of auxin-induced Ca2+ entry in plant cell suspensions to better understand the molecular mechanism of auxin-induced Ca2+ and to explore the physiological relevance of Ca2+ in auxin signal transduction. Using this approach, we defined a set of diverse, small molecules that interfere with auxin-induced Ca2+ entry. Based on annotated biological activities of the hit molecules, we found that auxin-induced Ca2+ signaling is, among others, highly sensitive to disruption of membrane proton gradients and the mammalian Ca2+ channel inhibitor bepridil. Whereas protonophores nonselectively inhibited auxin-induced and osmotic stress-induced Ca2+ signals, bepridil specifically inhibited auxin-induced Ca2+ We found evidence that bepridil severely alters vacuolar morphology and antagonized auxin-induced vacuolar remodeling. Further exploration of this plant-tailored collection of inhibitors will lead to a better understanding of auxin-induced Ca2+ entry and its relevance for auxin responses.Entities:
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Year: 2019 PMID: 30737267 PMCID: PMC6501068 DOI: 10.1104/pp.18.01393
Source DB: PubMed Journal: Plant Physiol ISSN: 0032-0889 Impact factor: 8.340