Protein kinase function and glutathionylation.

Anthony N. Anselmo, Melanie H. Cobb

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Intracellular reactive oxygen species are generated as a by-product of normal metabolic processes and can both damage cellular constituents and function as important signalling species. This signalling often involves changes in the thiol redox balance. As an antioxidant, glutathione serves in maintaining the reduced state of cellular protein thiol groups. The paper by Cross and Templeton appearing in this issue of the Biochemical Journal describes a mechanism by which glutathionylation plays a key role in the regulation of the kinase activity of MEKK1 [MAP (mitogen-activated protein kinase)/ERK (extracellular-signal-regulated kinase) kinase kinase; MAP3K] in response to oxidative stresses. This type of post-translational-modification glutathionylation may represent a general mechanism by which protein kinase function can be regulated.

Original languageEnglish (US)
JournalThe Biochemical journal
Volume381
Issue numberPt 3
StatePublished - 2004

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Protein Kinases
Phosphotransferases
Sulfhydryl Compounds
MAP Kinase Kinase Kinase 1
Oxidative stress
Extracellular Signal-Regulated MAP Kinases
Post Translational Protein Processing
Mitogen-Activated Protein Kinases
Oxidation-Reduction
Glutathione
Byproducts
Reactive Oxygen Species
Oxidative Stress
Antioxidants
Proteins

Cite this

Protein kinase function and glutathionylation. / Anselmo, Anthony N.; Cobb, Melanie H.

In: The Biochemical journal, Vol. 381, No. Pt 3, 2004.

Research output: Contribution to journalArticle

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