Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation.

S. G. Rhee, Y. S. Bae, S. R. Lee, J. Kwon

Research output: Contribution to journalReview articlepeer-review

578 Scopus citations

Abstract

Ligand-receptor interactions can generate the production of hydrogen peroxide (H(2)O(2)) in cells, the implications of which are becoming appreciated. Fluctuations in H(2)O(2) levels can affect the intracellular activity of key signaling components including protein kinases and protein phosphatases. Rhee et al. discuss recent findings on the role of H(2)O(2) in signal transduction. Specifically, H(2)O(2) appears to oxidize active site cysteines in phosphatases, thereby inactivating them. H(2)O(2) also can activate protein kinases; however, although the mechanism of activation for some kinases appears to be similar to that of phosphatase inactivation (cysteine oxidation), it is unclear how H(2)O(2) promotes increased activation of other kinases. Thus, the higher levels of intracellular phosphoproteins observed in cells most likely occur because of the concomitant inhibition of protein phosphatases and activation of protein kinases.

Original languageEnglish
Pages (from-to)PE1
JournalScience's STKE : signal transduction knowledge environment
Volume2000
Issue number53
DOIs
StatePublished - 10 Oct 2000

Fingerprint

Dive into the research topics of 'Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation.'. Together they form a unique fingerprint.

Cite this