Author:
Soler D. C.,Kowatz T.,Sloan A. E.,McCormick T. S.,Cooper K. D.,Stepanyan R.,Engel A.,Vahedi-Faridi A.
Abstract
AbstractThe inability to over-express Aquaporin 6 (AQP6) in the plasma membrane of heterologous cells has hampered efforts to further characterize the function of this aquaglyceroporin membrane protein at atomic detail using crystallographic approaches. Using an Aquaporin 3-tGFP Reporter (AGR) system we have identified a region within loop C of AQP6 that is responsible for severely hampering plasma membrane expression. Serine substitution corroborated that amino acids present within AQP6194–213 of AQP6 loop C contribute to intracellular endoplasmic reticulum (ER) retention. This intracellular retention signal may preclude proper plasma membrane trafficking and severely curtail expression of AQP6 in heterologous expression systems.
Publisher
Springer Science and Business Media LLC
Reference21 articles.
1. Vahedi-Faridi, A., Engel, A. Aquaporin structure and selectivity. in Aquaporins in Health and Disease: New Molecular Targets for Drug Discovery, 33–48. (CRC Press, 2016).
2. Gonen, T. & Walz, T. The structure of aquaporins. Q. Rev. Biophys. 39(4), 361–396 (2006).
3. Verkman, A. S. Mammalian aquaporins: Diverse physiological roles and potential clinical significance. Expert Rev. Mol. Med. 10, e13 (2008).
4. Wu, B. & Beitz, E. Aquaporins with selectivity for unconventional permeants. Cell Mol. Life Sci. 64(18), 2413–2421 (2007).
5. Heymann, J. B. & Engel, A. Aquaporins: Phylogeny, structure, and physiology of water channels. News Physiol. Sci. 14, 187–193 (1999).
Cited by
4 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献