Assay to visualize specific protein oxidation reveals spatio-temporal regulation of SHP2

Ryouhei Tsutsumi (), Jana Harizanova, Rabea Stockert, Katrin Schröder, Philippe I. H. Bastiaens and Benjamin G. Neel
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Ryouhei Tsutsumi: NYU Langone Health
Jana Harizanova: Max Planck Institute of Molecular Physiology
Rabea Stockert: Max Planck Institute of Molecular Physiology
Katrin Schröder: Goethe-University
Philippe I. H. Bastiaens: Max Planck Institute of Molecular Physiology
Benjamin G. Neel: NYU Langone Health

Nature Communications, 2017, vol. 8, issue 1, 1-14

Abstract: Abstract Reactive oxygen species are produced transiently in response to cell stimuli, and function as second messengers that oxidize target proteins. Protein-tyrosine phosphatases are important reactive oxygen species targets, whose oxidation results in rapid, reversible, catalytic inactivation. Despite increasing evidence for the importance of protein-tyrosine phosphatase oxidation in signal transduction, the cell biological details of reactive oxygen species-catalyzed protein-tyrosine phosphatase inactivation have remained largely unclear, due to our inability to visualize protein-tyrosine phosphatase oxidation in cells. By combining proximity ligation assay with chemical labeling of cysteine residues in the sulfenic acid state, we visualize oxidized Src homology 2 domain-containing protein-tyrosine phosphatase 2 (SHP2). We find that platelet-derived growth factor evokes transient oxidation on or close to RAB5+/ early endosome antigen 1− endosomes. SHP2 oxidation requires NADPH oxidases (NOXs), and oxidized SHP2 co-localizes with platelet-derived growth factor receptor and NOX1/4. Our data demonstrate spatially and temporally limited protein oxidation within cells, and suggest that platelet-derived growth factor-dependent “redoxosomes,” contribute to proper signal transduction.

Date: 2017
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DOI: 10.1038/s41467-017-00503-w

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