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Heterotrimeric Gα subunit from wheat (Triticum aestivum), GA3, interacts with the calcium-binding protein, Clo3, and the phosphoinositide-specific phospholipase C, PI-PLC1

Title:

Heterotrimeric Gα subunit from wheat (Triticum aestivum), GA3, interacts with the calcium-binding protein, Clo3, and the phosphoinositide-specific phospholipase C, PI-PLC1

Khalil, Hala Badr, Wang, Zhejun, Wright, Justin A., Ralevski, Alexandra, Donayo, Ariel O. and Gulick, Patrick (2011) Heterotrimeric Gα subunit from wheat (Triticum aestivum), GA3, interacts with the calcium-binding protein, Clo3, and the phosphoinositide-specific phospholipase C, PI-PLC1. Plant Molecular Biology, 77 (1-2). pp. 145-158. ISSN 0167-4412

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Official URL: http://dx.doi.org/10.1007/s11103-011-9801-1

Abstract

The canonical Gα subunit of the heterotrimeric G protein complex from wheat (Triticum aestivum), GA3, and the calcium-binding protein, Clo3, were revealed to interact both in vivo and in vitro and Clo3 was shown to enhance the GTPase activity of GA3. Clo3 is a member of the caleosin gene family in wheat with a single EF-hand domain and is induced during cold acclimation. Bimolecular Fluorescent Complementation (BiFC) was used to localize the interaction between Clo3 and GA3 to the plasma membrane (PM). Even though heterotrimeric G-protein signaling and Ca2+ signaling have both been shown to play a role in the response to environmental stresses in plants, little is known about the interaction between calcium-binding proteins and Gα. The GAP activity of Clo3 towards GA3 suggests it may play a role in the inactivation of GA3 as part of the stress response in plants. GA3 was also shown to interact with the phosphoinositide-specific phospholipase C, PI-PLC1, not only in the PM but also in the endoplasmic reticulum (ER). Surprisingly, Clo3 was also shown to interact with PI-PLC1 in the PM and ER. In vitro analysis of the protein–protein interaction showed that the interaction of Clo3 with GA3 and PI-PLC1 is enhanced by high Ca2+ levels. Three-way affinity characterizations with GA3, Clo3 and PI-PLC1 showed the interaction with Clo3 to be competitive, which suggests that Clo3 may play a role in the Ca2+-triggered feedback regulation of both GA3 and PI-PLC1. This hypothesis was further supported by the demonstration that Clo3 has GAP activity with GA3.

Divisions:Concordia University > Faculty of Arts and Science > Biology
Item Type:Article
Refereed:Yes
Authors:Khalil, Hala Badr and Wang, Zhejun and Wright, Justin A. and Ralevski, Alexandra and Donayo, Ariel O. and Gulick, Patrick
Journal or Publication:Plant Molecular Biology
Date:2011
Digital Object Identifier (DOI):10.1007/s11103-011-9801-1
ID Code:36111
Deposited By: ANDREA MURRAY
Deposited On:28 Nov 2011 20:02
Last Modified:18 Jan 2018 17:36
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