Identification of Post Translational Modification Sites in Dynamin-related Protein 1

摘要

In the present study, we used high-accracy bottom-up mass spectrometry analysis to assess the PTMs of Drp1 protein treated in different biological conditions New PTMs were identified in Drp1 protein. In Drp1 protein treated with DMSO, one Ser and one Tyr were phosphorylated; One Tyr and one Cys were nitrosylated. In Drp1 protein treated with STS, only one Tyr was phosphorylated; two Lysines were ubiquitinated; One Tyr and one Cys were nitrosylated. All proteins were unambiguously identified with better than 90percent sequence coverage.