S-Glutathionylation of Cryptic Cysteines Enhances Titin Elasticity by Blocking Protein Folding

• Published in: Cell Vol. 156; no. 6; pp. 1235 - 1246
• Main Authors: Alegre-Cebollada, Jorge, Kosuri, Pallav, Giganti, David, Eckels, Edward, Rivas-Pardo, Jaime Andrés, Hamdani, Nazha, Warren, Chad M., Solaro, R. John, Linke, Wolfgang A., Fernández, Julio M.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 13.03.2014
• Subjects: Biomechanical Phenomena; blood; cardiomyocytes; Connectin - chemistry; Connectin - metabolism; cysteine; Cysteine - metabolism; Elasticity; etiology; extensibility; Glutaredoxins - metabolism; heart diseases; Humans; immunoglobulin A; Models, Molecular; Myocytes, Cardiac - cytology; Myocytes, Cardiac - metabolism; post-translational modification; Protein Folding; Protein Processing, Post-Translational; Protein Structure, Tertiary

The giant elastic protein titin is a determinant factor in how much blood fills the left ventricle during diastole and thus in the etiology of heart disease. Titin has been identified as a target of S-glutathionylation, an end product of the nitric-oxide-signaling cascade that increases cardiac musc...