Structural highlights
Function
[AQP5_HUMAN] Forms a water-specific channel. Implicated in the generation of saliva, tears, and pulmonary secretions.
Publication Abstract from PubMed
Aquaporin membrane protein channels mediate cellular water flow. Human aquaporin 5 (AQP5) is highly expressed in the respiratory system and secretory glands where it facilitates the osmotically-driven generation of pulmonary secretions, saliva, sweat and tears. Dysfunctional trafficking of AQP5 has been implicated in several human disease states, including Sjogren's syndrome, bronchitis and cystic fibrosis. In order to investigate how the plasma membrane expression levels of AQP5 are regulated, we studied real-time translocation of GFP-tagged AQP5 in HEK293 cells. We show that AQP5 plasma membrane abundance in transfected HEK293 cells is rapidly and reversibly regulated by at least three independent mechanisms involving phosphorylation at Ser156, protein kinase A activity and extracellular tonicity. The crystal structure of a Ser156 phosphomimetic mutant indicates that its involvement in regulating AQP5 membrane abundance is not mediated by a conformational change of the carboxy-terminus. We suggest that together these pathways regulate cellular water flow.
Plasma Membrane Abundance of Human Aquaporin 5 Is Dynamically Regulated by Multiple Pathways.,Kitchen P, Oberg F, Sjohamn J, Hedfalk K, Bill RM, Conner AC, Conner MT, Tornroth-Horsefield S PLoS One. 2015 Nov 16;10(11):e0143027. doi: 10.1371/journal.pone.0143027., eCollection 2015. PMID:26569106[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kitchen P, Oberg F, Sjohamn J, Hedfalk K, Bill RM, Conner AC, Conner MT, Tornroth-Horsefield S. Plasma Membrane Abundance of Human Aquaporin 5 Is Dynamically Regulated by Multiple Pathways. PLoS One. 2015 Nov 16;10(11):e0143027. doi: 10.1371/journal.pone.0143027., eCollection 2015. PMID:26569106 doi:http://dx.doi.org/10.1371/journal.pone.0143027
