In this study, we performed a mass spectrometry (MS)-based phosphoproteomics to conduct a global and dynamic phosphoproteome profiling across five time points of BR treatment in the period between 5 min and 12 h.  MS coupling with phosphopeptide enrichment techniques has become the powerful tool for profiling protein phosphorylation.  However, MS-based methods tend to have data consistency and coverage issues.  The time-dependent gene ontology (GO) analysis shows the transition of biological processes from signaling transduction to morphogenesis and stress response.  The phosphoproteins and phosphosites identified in our study provide a useful dataset for revealing signaling networks of BR regulation, and also expanded our knowledge of protein phosphorylation modification in plants as well as further deal to solve the plant growth problems.
MS
MS coupling with phosphopeptide enrichment techniques has become the powerful tool for profiling protein phosphorylation. 
phosphopeptide enrichment techniques
To address these issues, bioinformatics approaches were used to complement the non-detected proteins and recover the dynamics of phosphorylation events.



bioinformatics approaches
The analysis by using Motif-X was performed to identify 15 enriched motifs, 11 of which correspond to 6 known kinase families. 
Motif-X