Key laboratory of Cellular Engineering and Germplasm Innovation

Port-of-Spain, Trinidad and Tobago

Key laboratory of Cellular Engineering and Germplasm Innovation

Port-of-Spain, Trinidad and Tobago
SEARCH FILTERS
Time filter
Source Type

Zhao X.,Key laboratory of Cellular Engineering and Germplasm Innovation | Wang M.,Key laboratory of Cellular Engineering and Germplasm Innovation | Quan T.,Key laboratory of Cellular Engineering and Germplasm Innovation | Xia G.,Key laboratory of Cellular Engineering and Germplasm Innovation
Plant Signaling and Behavior | Year: 2012

In our previous study, we found wheat TaCHP confers salt tolerance through regulating salt responsive signaling pathways. TaCHP possesses three divergent C1 domains that can specifically bind to phospholipid signaling molecule diacylglycerol (DAG) in animal cells, and most of proteins with this domain have kinase activity. Here, we found that TaCHP localizes both at cytoplasmatic membrane and in nuclei; it has no kinase activity but transcriptional activation activity, and the latter owes to C-terminal two C1 domains. TaCHP transcription was reduced by H 2O 2 application, but its ectopic expression in Arabidopsis improved both ROS production and scavenging capacity, and enhanced tolerance to H 2O 2 application. We suggest that TaCHP serve as both a transcription factor and a putative DAG binding protein to confer salt tolerance in part through improving ROS scavenging capacity, and that it is a component of the cross-talk machinery in the phospholipids-ROS-salt responsive signaling pathways. © 2012 Landes Bioscience.


Dong W.,Key Laboratory of Cellular Engineering and Germplasm Innovation | Lv H.,Key Laboratory of Cellular Engineering and Germplasm Innovation | Xia G.,Key Laboratory of Cellular Engineering and Germplasm Innovation | Wang M.,Key Laboratory of Cellular Engineering and Germplasm Innovation
Plant Signaling and Behavior | Year: 2012

Diacylglycerol (DAG) is an important signaling phospholipid in animals, specifically binding to the C1 domain of proteins such as protein kinase C. In most plant species, however, DAG is present at low abundance, and no interacting proteins have yet been identified. As a result, it has been proposed that the signaling function of DAG has been discarded by plants during their evolution. In this mini-review, we summarize the accumulating experimental evidence which supports that notion that changes in DAG content in response to particular cues are a feature of plant cells. This behavior suggests that DAG does indeed act as a signaling molecule during plant development and in response to certain environmental stimuli. © 2012 Landes Bioscience.

Loading Key laboratory of Cellular Engineering and Germplasm Innovation collaborators
Loading Key laboratory of Cellular Engineering and Germplasm Innovation collaborators