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Decoding Post-Translational Modification Crosstalk With Proteomics
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DOI：10.1016/j.mcpro.2021.100129.png)
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Abstract
En 中文
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.
Keywords:
SPECTROMETRY ENABLES CHARACTERIZATION
MASS-SPECTROMETRY
TOP-DOWN
FUNCTIONAL ASSOCIATIONS
GLOBAL ANALYSIS
PTM CROSSTALK
HISTONE H3R2
PHOSPHORYLATION
UBIQUITIN
REVEALS
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