Proteomics

Dataset Information

0

Sequential enrichment of phosphorylation on reversibly oxidized proteoforms – part 3


ABSTRACT: Post-translational modifications (PTMs) are necessary for the regulation of critical processes including metabolism, signaling, and overall homeostasis. While proteins PTMs have been largely investigated independently in bottom-up proteomics methodologies, examination into how different PTMs interact, or crosstalk, will reveal a more complete understanding of the reciprocity of signaling cascades across numerous pathways. Combinatorial reversible thiol oxidation and phosphorylation in eukaryotes is largely recognized, but rigorous approaches for experimental verification are underdeveloped and must be advanced to begin meaningful definition of crosstalk in targeted pathway and systems biology research. Herein, we applied protein-level enrichment of reversibly oxidized proteoforms in Chlamydomonas reinhardtii with subsequent phosphopeptide analysis to determine the extent of phosphorylation in the redox thiol proteome.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Chlamydomonas Reinhardtii

SUBMITTER: Evan McConnell  

LAB HEAD: Leslie M. Hicks

PROVIDER: PXD009038 | Pride | 2018-04-23

REPOSITORIES: Pride

altmetric image

Publications

The phosphorylated redox proteome of Chlamydomonas reinhardtii: Revealing novel means for regulation of protein structure and function.

McConnell Evan W EW   Werth Emily G EG   Hicks Leslie M LM  

Redox biology 20180404


Post-translational modifications (PTMs) are covalent modifications to protein residues which may alter both conformation and activity, thereby modulating signaling and metabolic processes. While PTMs have been largely investigated independently, examination into how different modification interact, or crosstalk, will reveal a more complete understanding of the reciprocity of signaling cascades across numerous pathways. Combinatorial reversible thiol oxidation and phosphorylation in eukaryotes is  ...[more]

Similar Datasets

2018-04-23 | PXD008370 | Pride
2018-04-23 | PXD008371 | Pride
| S-EPMC2248312 | biostudies-literature
2023-03-10 | PXD020270 | Pride
| S-EPMC3289665 | biostudies-literature
2019-12-10 | PXD011525 | Pride
| S-EPMC2981573 | biostudies-literature
| S-EPMC5666389 | biostudies-literature
2020-03-30 | PXD014381 | Pride
2019-03-19 | PXD009693 | Pride