Transduction of redox signaling by electrophile-protein reactions
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Transduction of redox signaling by electrophile-protein reactions. / Rudolph, Tanja K; Freeman, Bruce A.
in: SCIENCE SIGNALING, Jahrgang 2, Nr. 90, 29.09.2009, S. 7.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Review › Forschung
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TY - JOUR
T1 - Transduction of redox signaling by electrophile-protein reactions
AU - Rudolph, Tanja K
AU - Freeman, Bruce A
PY - 2009/9/29
Y1 - 2009/9/29
N2 - Over the last 50 years, the posttranslational modification (PTM) of proteins has emerged as a central mechanism for cells to regulate metabolism, growth, differentiation, cell-cell interactions, and immune responses. By influencing protein structure and function, PTM leads to a multiplication of proteome diversity. Redox-dependent PTMs, mediated by environmental and endogenously generated reactive species, induce cell signaling responses and can have toxic effects in organisms. PTMs induced by the electrophilic by-products of redox reactions most frequently occur at protein thiols; other nucleophilic amino acids serve as less favorable targets. Advances in mass spectrometry and affinity-chemistry strategies have improved the detection of electrophile-induced protein modifications both in vitro and in vivo and have revealed a high degree of amino acid and protein selectivity of electrophilic PTM. The identification of biological targets of electrophiles has motivated further study of the functional impact of various PTM reactions on specific signaling pathways and how this might affect organisms.
AB - Over the last 50 years, the posttranslational modification (PTM) of proteins has emerged as a central mechanism for cells to regulate metabolism, growth, differentiation, cell-cell interactions, and immune responses. By influencing protein structure and function, PTM leads to a multiplication of proteome diversity. Redox-dependent PTMs, mediated by environmental and endogenously generated reactive species, induce cell signaling responses and can have toxic effects in organisms. PTMs induced by the electrophilic by-products of redox reactions most frequently occur at protein thiols; other nucleophilic amino acids serve as less favorable targets. Advances in mass spectrometry and affinity-chemistry strategies have improved the detection of electrophile-induced protein modifications both in vitro and in vivo and have revealed a high degree of amino acid and protein selectivity of electrophilic PTM. The identification of biological targets of electrophiles has motivated further study of the functional impact of various PTM reactions on specific signaling pathways and how this might affect organisms.
KW - Animals
KW - Cysteine/chemistry
KW - Electrochemistry
KW - Humans
KW - Models, Biological
KW - Models, Molecular
KW - Oxidation-Reduction
KW - Protein Processing, Post-Translational
KW - Proteins/chemistry
KW - Signal Transduction/physiology
U2 - 10.1126/scisignal.290re7
DO - 10.1126/scisignal.290re7
M3 - SCORING: Review article
C2 - 19797270
VL - 2
SP - 7
JO - SCI SIGNAL
JF - SCI SIGNAL
SN - 1945-0877
IS - 90
ER -