AtaGenix Custom Phospho-specific Antibody Service Facilitates the Discovery of a Novel Mechanism of G Protein-Mediated Growth Regulation in Tomato

Research Background

Plant vigour directly determines crop yield and photosynthetic efficiency, representing a core focus of global food security and high-yield breeding research. The G protein signalling pathway, a key regulator of plant growth, photosynthesis, and productivity, remains insufficiently understood at the molecular level.

A recent Cell Reports publication from Zhejiang University, titled “Functional divergence of G protein γ subunits drives plant vigour and improvement through the CPK28–PIP1;2 pathway in tomato,” revealed that the G protein γ subunit GGC1 underwent positive selection during tomato domestication. The study demonstrated that GGC1 acts as a negative regulator of plant growth and photosynthesis by suppressing CPK28-mediated phosphorylation of PIP1;2 at Thr172, thereby identifying a previously uncharacterised G protein–mediated signalling cascade, the GGC1–CPK28–PIP1;2 axis, which plays a crucial role in crop growth regulation.

Client Requirements

To verify the regulatory mechanism by which GGC1 influences CPK28-mediated PIP1;2 phosphorylation, the research team required an antibody capable of specifically recognising PIP1;2 phosphorylated at Thr172, suitable for quantitative detection and Western blot validation in tomato mutant samples.

Technical Challenges

1. Site specificity: The antibody needed to distinguish phosphorylation at Thr172 from neighbouring Tyr171.

2. Species specificity: It was essential that the antibody recognised PIP1;2 from tomato (Solanum lycopersicum).

3. Low abundance detection: Phosphorylated proteins are generally present at low levels in plant tissues, necessitating an antibody with high affinity and sensitivity.

AtaGenix Custom Phospho-specific Antibody Solution

To meet the research requirements, AtaGenix conducted sequence analysis of PIP1;2 and evaluated the conservation surrounding the phosphorylation site. A synthetic phosphopeptide containing pThr172 was precisely designed, and the differentiation from the corresponding non-phosphorylated peptide was optimised. A multi-stage process involving immunisation, serum purification, and affinity purification was used to ensure the antibody specifically recognised the phosphorylated form of PIP1;2.

Contribution and Impact

This study provides the first evidence that GGC1 regulates photosynthetic efficiency and plant vigour by suppressing CPK28-mediated phosphorylation of PIP1;2 at Thr172. The anti-PIP1;2 (pT172) phospho-specific antibody custom-developed by AtaGenix provided critical experimental evidence, enabling the researchers to uncover a new molecular pathway governing crop growth.

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