Related Experiment Video
Updated: Mar 22, 2026

13:02
Arabidopsis thaliana Polar Glycerolipid Profiling by Thin Layer Chromatography TLC Coupled with Gas-Liquid Chromatography GLC
Published on: March 18, 2011
38.2K
Phospholipases as GTPase activity accelerating proteins (GAPs) in plants
1a Donald Danforth Plant Science Center , St. Louis , MO , USA.
Plant Signaling & Behavior
|April 29, 2016
Summary
Phospholipase Dα1 (PLDα1) is a newly identified GTPase accelerating protein (GAP) in plants. This finding reveals that PLDα1, alongside RGS proteins, regulates active G-protein signaling levels.
Area of Science:
- Plant molecular biology
- Cell signaling
Background:
- GTPase accelerating proteins (GAPs) regulate G-protein signaling by controlling GTP hydrolysis on Gα proteins.
- Previously, only Regulator of G-protein Signaling (RGS) proteins were recognized as plant GAPs.
- GAPs are crucial for the timing, amplitude, and reactivation of the G-protein signaling cycle.
Purpose of the Study:
- To identify novel GAPs in plant signaling pathways.
- To investigate the role of Phospholipase Dα1 (PLDα1) as a potential GAP.
- To understand the combined function of PLDα1 and RGS proteins in regulating G-protein activity.
Main Methods:
- Biochemical assays to measure GTPase accelerating activity.
- In vitro and in vivo experiments to assess protein interactions.
- Analysis of G-protein signaling components in plant systems.
Main Results:
- Phospholipase Dα1 (PLDα1) demonstrates bona fide GTPase accelerating protein (GAP) activity in plants.
- PLDα1 functions alongside RGS proteins to modulate active Gα protein levels.
- This dual regulation impacts the G-protein signaling cycle.
Conclusions:
- PLDα1 represents a novel class of plant GAPs.
- The interplay between PLDα1 and RGS proteins provides a more comprehensive understanding of G-protein signaling regulation in plants.
- This discovery expands the known regulators of plant G-protein pathways.
Related Concept Videos
IP3/DAG Signaling Pathway
15.8K
Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
15.8K
GTPases and their Regulation
10.3K
Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒ small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins,...
Large G-proteins,...
10.3K
GTPases and their Regulation
3.2K
3.2K
Phosphoinositides and PIPs
10.5K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
10.5K
Small GTPases - Ras and Rho
5.7K
Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
Three regulatory proteins control their activity:
5.7K
Activation and Inactivation of G Proteins
12.3K
Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
12.3K

