The C2-domain protein QUIRKY and the receptor-like kinase STRUBBELIG localize to plasmodesmata and mediate tissue morphogenesis in Arabidopsis thaliana

Tissue morphogenesis in plants requires communication between cells, a process involving the trafficking of molecules through plasmodesmata (PD). PD conductivity is regulated by endogenous and exogenous signals. However, the underlying signaling mechanisms remain enigmatic. In Arabidopsis, signal tr...

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Main Authors: Vaddepalli, Ponduranga Vara Prasad (Author) , Hillmer, Stefan (Author) , Robinson, David G. (Author)
Format: Article (Journal)
Language:English
Published: August 26, 2014
In: Development
Year: 2014, Volume: 141, Issue: 21, Pages: 4139-4148
ISSN:1477-9129
DOI:10.1242/dev.113878
Online Access:Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1242/dev.113878
Verlag, Volltext: http://dev.biologists.org/content/141/21/4139
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Author Notes:Prasad Vaddepalli, Anja Herrmann, Lynette Fulton, Maxi Oelschner, Stefan Hillmer, Thomas F. Stratil, Astrid Fastner, Ulrich Z. Hammes, Thomas Ott, David G. Robinson, Kay Schneitz
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Summary:Tissue morphogenesis in plants requires communication between cells, a process involving the trafficking of molecules through plasmodesmata (PD). PD conductivity is regulated by endogenous and exogenous signals. However, the underlying signaling mechanisms remain enigmatic. In Arabidopsis, signal transduction mediated by the receptor-like kinase STRUBBELIG (SUB) contributes to inter-cell layer signaling during tissue morphogenesis. Previous analysis has revealed that SUB acts non-cell-autonomously suggesting that SUB controls tissue morphogenesis by participating in the formation or propagation of a downstream mobile signal. A genetic screen identified QUIRKY (QKY), encoding a predicted membrane-anchored C2-domain protein, as a component of SUB signaling. Here, we provide further insight into the role of QKY in this process. We show that like SUB, QKY exhibits non-cell-autonomy when expressed in a tissue-specific manner and that non-autonomy of QKY extends across several cells. In addition, we report on localization studies indicating that QKY and SUB localize to PD but independently of each other. FRET-FLIM analysis suggests that SUB and QKY are in close contact at PD in vivo. We propose a model where SUB and QKY interact at PD to promote tissue morphogenesis, thereby linking RLK-dependent signal transduction and intercellular communication mediated by PD.
Item Description:Gesehen am 13.07.2017
Physical Description:Online Resource
ISSN:1477-9129
DOI:10.1242/dev.113878