Ca2+-dependent phosphoregulation of the plasma membrane Ca2+-ATPase ACA8 modulates stimulus-induced calcium signatures

© The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 68(2017), 12 vom: 01. Juni, Seite 3215-3230
1. Verfasser: Costa, Alex (VerfasserIn)
Weitere Verfasser: Luoni, Laura, Marrano, Claudia Adriana, Hashimoto, Kenji, Köster, Philipp, Giacometti, Sonia, De Michelis, Maria Ida, Kudla, Jörg, Bonza, Maria Cristina
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2017
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Arabidopsis thaliana CBL-interacting protein kinases Ca2+ signature calcineurin B-like protein phosphorylation plasma membrane Ca2+-ATPase Arabidopsis Proteins Aca8 protein, Arabidopsis EC 7.2.2.10 mehr... Calcium-Transporting ATPases Calcium SY7Q814VUP
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100 1 |a Costa, Alex  |e verfasserin  |4 aut 
245 1 0 |a Ca2+-dependent phosphoregulation of the plasma membrane Ca2+-ATPase ACA8 modulates stimulus-induced calcium signatures 
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520 |a © The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology. 
520 |a Ca2+ signals are transient, hence, upon a stimulus-induced increase in cytosolic Ca2+ concentration, cells have to re-establish resting Ca2+ levels. Ca2+ extrusion is operated by a wealth of transporters, such as Ca2+ pumps and Ca2+/H+ antiporters, which often require a rise in Ca2+ concentration to be activated. Here, we report a regulatory fine-tuning mechanism of the Arabidopsis thaliana plasma membrane-localized Ca2+-ATPase isoform ACA8 that is mediated by calcineurin B-like protein (CBL) and CBL-interacting protein kinase (CIPK) complexes. We show that two CIPKs (CIPK9 and CIPK14) are able to interact with ACA8 in vivo and phosphorylate it in vitro. Transient co-overexpression of ACA8 with CIPK9 and the plasma membrane Ca2+ sensor CBL1 in tobacco leaf cells influences nuclear Ca2+ dynamics, specifically reducing the height of the second peak of the wound-induced Ca2+ transient. Stimulus-induced Ca2+ transients in mature leaves and seedlings of an aca8 T-DNA insertion line exhibit altered dynamics when compared with the wild type. Altogether our results identify ACA8 as a prominent in vivo regulator of cellular Ca2+ dynamics and reveal the existence of a Ca2+-dependent CBL-CIPK-mediated regulatory feedback mechanism, which crucially functions in the termination of Ca2+ signals 
650 4 |a Journal Article 
650 4 |a Arabidopsis thaliana 
650 4 |a CBL-interacting protein kinases 
650 4 |a Ca2+ signature 
650 4 |a calcineurin B-like protein 
650 4 |a phosphorylation 
650 4 |a plasma membrane Ca2+-ATPase 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a Aca8 protein, Arabidopsis  |2 NLM 
650 7 |a EC 7.2.2.10  |2 NLM 
650 7 |a Calcium-Transporting ATPases  |2 NLM 
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650 7 |a Calcium  |2 NLM 
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700 1 |a Luoni, Laura  |e verfasserin  |4 aut 
700 1 |a Marrano, Claudia Adriana  |e verfasserin  |4 aut 
700 1 |a Hashimoto, Kenji  |e verfasserin  |4 aut 
700 1 |a Köster, Philipp  |e verfasserin  |4 aut 
700 1 |a Giacometti, Sonia  |e verfasserin  |4 aut 
700 1 |a De Michelis, Maria Ida  |e verfasserin  |4 aut 
700 1 |a Kudla, Jörg  |e verfasserin  |4 aut 
700 1 |a Bonza, Maria Cristina  |e verfasserin  |4 aut 
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773 1 8 |g volume:68  |g year:2017  |g number:12  |g day:01  |g month:06  |g pages:3215-3230 
856 4 0 |u http://dx.doi.org/10.1093/jxb/erx162  |3 Volltext 
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