Review
Decoding Post-Translational Modification Crosstalk With Proteomics

https://doi.org/10.1016/j.mcpro.2021.100129Get rights and content
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Highlights

  • Description of basic modules and different modes of PTM crosstalk.

  • Overview of current proteomic methods to identify and infer PTM crosstalk.

  • Discussion of large-scale approaches to characterize functional PTM crosstalk.

  • Future directions and potential proteomic methods for elucidating PTM crosstalk.

Abstract

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

post-translational modification
proteomics
crosstalk
mass spectrometry

Abbreviations

IMAC
immobilized metal ion affinity chromatography
MS
mass spectrometry
PTM
post-translational modification

Cited by (0)

Present address for Samuel W. Entwisle: Department of Genetics, Harvard Medical School, Boston, Massachusetts, USA.

These authors contributed equally to this work.