期刊
MOLECULAR & CELLULAR PROTEOMICS
卷 20, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.mcpro.2021.100129
关键词
-
资金
- NIH [R35GM119536, R01AG056359, R01NS098329, RM1HG010461]
- Human Frontiers Science Program [RGP0034/2018]
- W. M. Keck Foundation
- Swiss National Science Foundation [P400PB_194379]
Post-translational modifications (PTMs) play a crucial role in regulating protein functions and diversifying the proteome. PTM crosstalk, the interaction between multiple PTMs on the same or different proteins, has been elucidated through advanced proteomic technologies, mass spectrometry instrumentation, and bioinformatics, providing insights into the functional consequences of these interactions.
Post-translational modification (PTM) of proteins allows cells to regulate protein functions, transduce signals and respond to perturbations. PTMs expand protein functionality and diversity, which leads to increased proteome complexity. PTM crosstalk describes the combinatorial action of multiple PTMs on the same or on different proteins for higher order regulation. Here we review how recent advances in proteomic technologies, mass spectrometry instrumentation, and bioinformatics spurred the proteome-wide identification of PTM crosstalk through measurements of PTM sites. We provide an overview of the basic modes of PTM crosstalk, the proteomic methods to elucidate PTM crosstalk, and approaches that can inform about the functional consequences of PTM crosstalk.
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