Regulation of PTP1B via Glutathionylation of the Active Site Cysteine 215

• Published in: Biochemistry (Easton) Vol. 38; no. 20; pp. 6699 - 6705
• Main Authors: Barrett, William C., DeGnore, Jon P., König, Simone, Fales, Henry M., Keng, Yen-Fang, Zhang, Zhong-Yin, Yim, Moon B., Chock, P. Boon
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 18.05.1999
• Subjects: Amino Acid Sequence; Binding Sites; Cysteine - chemistry; Cysteine - metabolism; Dithionitrobenzoic Acid - chemistry; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Glutathione - chemistry; Glutathione - metabolism; Glutathione - physiology; Glutathione Disulfide - chemistry; Glutathione Disulfide - metabolism; Glutathione Disulfide - physiology; Humans; Kinetics; Mass Spectrometry; Molecular Sequence Data; Oxidation-Reduction; Protein Tyrosine Phosphatases - antagonists & inhibitors; Protein Tyrosine Phosphatases - chemistry; Protein Tyrosine Phosphatases - metabolism; Titrimetry

The reversible regulation of protein tyrosine phosphatase is an important mechanism in processing signal transduction and regulating cell cycle. Recent reports have shown that the active site cysteine residue, Cys215, can be reversibly oxidized to a cysteine sulfenic derivative (Denu and Tanner, 199...