On April 28, 2020, Chen Yanmei, a team from the State Key Laboratory of plant physiology and biochemistry, School of Bioscience, China Agricultural University, published a research paper entitled "mass spectrum untangles plant membrane protein signaling networks" online at trends in plant science.
Membrane receptors, kinases and transporters communicate with intracellular processes through protein-protein interaction networks. Despite advances in separation and analysis techniques, characterization of plant PM proteins, especially hydrophobic proteins, remains challenging.
The rapid progress of MS instrument and data analysis has made significant progress in deciphering membrane proteome and mapping protein interaction partners, so that people have a better understanding of PM protein complex.
Analysis of membrane protein phosphorylation under specific cell conditions is essential to elucidate the molecular mechanisms of signal sensing, transport and metabolism. Phosphorylation proteomics allows unbiased localization and site-specific quantification of protein phosphorylation in vivo, thus contributing to the anatomic membrane signal network.
Plasma membrane (PMS), as the main cell checkpoint, is used to sense signals and control solute transport. Membrane proteins communicate with intracellular processes through protein interaction networks. Decryption of these signal networks provides key information for cell regulation in vivo. Large scale proteomics can systematically characterize membrane proteome, identify ligand receptor pairs and elucidate signals from membrane. In this review, we reviewed the recent progress of proteomics based on mass spectrometry (MS) in determining membrane signaling pathways. We are particularly concerned with current techniques for the analysis of membrane protein phosphorylation and interaction, and how these proteins relate to downstream changes in gene expression, metabolism, and physiology.