期刊
FRONTIERS IN MOLECULAR NEUROSCIENCE
卷 10, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fnmol.2017.00167
关键词
cellular redoxstasis; cysteine mutation; signaling pathways; disulfide bonding; protein misfolding
资金
- Fondazione Cariplo [2013-0967]
- EDY [PCOFUND-GA-2010-267264 INVEST]
- RS AIRC [IG14559]
- Fondazione Banca del Monte di Lombardia Fondazione Cariplo [2015-0591]
- Ministero della Salute [PE-2011-02352286]
- Telethon [GGP15059]
Thiol groups can undergo numerous modifications, making cysteine a unique molecular switch. Cysteine plays structural and regulatory roles as part of proteins or glutathione, contributing to maintain redox homeostasis and regulate signaling within and amongst cells. Not surprisingly therefore, cysteines are associated with many hereditary and acquired diseases. Mutations in the primary protein sequence (gain or loss of a cysteine) are most frequent in membrane and secretory proteins, correlating with the key roles of disulfide bonds. On the contrary, in the cytosol and nucleus, aberrant post-translational oxidative modifications of thiol groups, reflecting redox changes in the surrounding environment, are a more frequent cause of dysregulation of protein function. This essay highlights the regulatory functions performed by protein cysteine residues and provides a framework for understanding how mutation and/or (in) activation of this key amino acid can cause disease.
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