Protein tyrosine phosphorylation and reversible oxidation: two cross-talking posttranslation modifications

Area of Science:

• Cellular Biology
• Biochemistry
• Signal Transduction

Background:

• Redox-dependent posttranslational protein modification is a critical signaling system.
• Reactive oxygen species act as intracellular signal transducers.
• The interplay between phosphorylation and redox signaling is increasingly recognized.

Purpose of the Study:

• To review the cross-talk between tyrosine phosphorylation and thiol oxidation.
• To elucidate the opposing effects of these modifications on protein tyrosine phosphatases (PTPs) and protein tyrosine kinases (PTKs).
• To discuss the integrated function of PTPs and PTKs in cellular processes like proliferation and motility.

Main Methods:

• Literature review focusing on the interplay between phosphorylation and redox-dependent modifications.
• Analysis of studies investigating the effects on PTPs and PTKs.
• Synthesis of findings on convergent and divergent features of integrated signaling.

Main Results:

• Tyrosine phosphorylation often correlates with enzyme activation.
• Thiol oxidation typically leads to PTP inactivation and PTK superactivation.
• Both modifications occur concurrently during growth factor-induced cell proliferation and motility.

Conclusions:

• The cross-talk between phosphorylation and redox signaling is a dynamic and conserved mechanism.
• Opposing effects on PTPs and PTKs highlight a complex regulatory network.
• Integrated PTP and PTK function is crucial for cellular responses to external stimuli.