The Quantitative Biotinylproteomics Studies Reveal a WInd-Related Kinase 1 (WIRK1) Functioning as An Early Signaling Component in Wind-induced Thigmomorphogenesis and Gravitropism

Mol Cell Proteomics. 2024 Feb 14:100738. doi: 10.1016/j.mcpro.2024.100738. Online ahead of print.ABSTRACTWind is one of the most prevalent environmental forces entraining plants to develop various mechano-responses, collectively called thigmomorphogenesis. Largely unknown is how plants transduce these versatile wind force signals downstream to nuclear events and to the development of thigmomorphogenic phenotype or anemotropic response. To identify molecular components at the early steps of the wind force signaling, two mechanical signaling-related phosphoproteins, identified from our previous phosphoproteomic study of Arabidopsis touch response, mitogen-activated protein kinase kinase 1 (MKK1) and 2 (MKK2) were selected for performing in planta TurboID (ID)-based proximity-labeling (PL) proteomics. This quantitative biotinylproteomics was separately performed on MKK1-ID and MKK2-ID transgenic plants, respectively, using the genetically engineered TurboID biotin ligase expression transgenics as a universal control. This PTM proteomics successfully identified 11 and 71 MKK1 and MKK2 interactors, respectively. Biotin occupancy ratio (BOR) was found to be an alternative parameter to measure the specificity of bait fusion protein toward the target interactor. Bioinformatics analysis of these biotinylprotein data also found that TurboID biotin ligase favorably label the loop region of target proteins. A WInd-Related Kinase 1 (WIRK1), previously known as Raf-like kinase 36 (RAF 36),...
Source: Molecular and Cellular Proteomics : MCP - Category: Molecular Biology Authors: Source Type: research