| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8295354 | Biochemical and Biophysical Research Communications | 2018 | 6 Pages |
Abstract
Chloride intracellular channels (CLICs) exist in soluble and membrane bound forms. We have determined the crystal structure of soluble Clic2 from the euryhaline teleost fish Oreochromis mossambicus. Structural comparison of tilapia and human CLIC2 with other CLICs shows that these proteins are highly conserved. We have also compared the expression levels of clic2 in selected osmoregulatory organs of tilapia, acclimated to freshwater, seawater and hypersaline water. Structural conservation of vertebrate CLICs implies that they might play conserved roles. Also, tissue-specific responsiveness of clic2 suggests that it might be involved in iono-osmoregulation under extreme conditions in tilapia.
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Authors
Jiao Zeng, Zhengjun Li, Eei Yin Lui, Siew Hong Lam, Kunchithapadam Swaminathan,