Chapter title |
The STIM-Orai Pathway: Regulation of STIM and Orai by Thiol Modifications
|
---|---|
Chapter number | 6 |
Book title |
Store-Operated Ca²⁺ Entry (SOCE) Pathways
|
Published in |
Advances in experimental medicine and biology, January 2017
|
DOI | 10.1007/978-3-319-57732-6_6 |
Pubmed ID | |
Book ISBNs |
978-3-31-957731-9, 978-3-31-957732-6
|
Authors |
Barbara A. Niemeyer |
Abstract |
Cysteines are among the least abundant amino acids found in proteins. Due to their unique nucleophilic thiol group, they are able to undergo a broad range of chemical modifications besides their known role in disulfide formation, such as S-sulfenylation (-SOH), S-sulfinylation (-SO(2)H), S-sufonylation (-SO(3)H), S-glutathionylation (-SSG), and S-sulfhydration (-SSH), among others. These posttranslational modifications can be irreversible and act as transitional modifiers or as reversible on-off switches for the function of proteins. Disturbances of the redox homeostasis, for example, in situations of increased oxidative stress, can contribute to a range of diseases. Because Ca(2+) signaling mediated by store-operated calcium entry (SOCE) is involved in a plethora of cellular responses, the cross-talk between reactive oxygen species (ROS) and Ca(2+) is critical for homeostatic control. Identification of calcium regulatory protein targets of thiol redox modifications is needed to understand their role in biology and disease. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 9 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Professor > Associate Professor | 1 | 11% |
Student > Bachelor | 1 | 11% |
Professor | 1 | 11% |
Student > Ph. D. Student | 1 | 11% |
Student > Master | 1 | 11% |
Other | 1 | 11% |
Unknown | 3 | 33% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 5 | 56% |
Agricultural and Biological Sciences | 1 | 11% |
Unknown | 3 | 33% |