Protein kinase function and glutathionylation.

Anthony N. Anselmo, Melanie H. Cobb

Research output: Contribution to journalComment/debate

26 Scopus citations

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)
Pages (from-to)e1-2
JournalThe Biochemical journal
Volume381
Issue numberPt 3
DOIs
StatePublished - Aug 1 2004

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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