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5C5X

CRYSTAL STRUCTURE OF THE S156E MUTANT OF HUMAN AQUAPORIN 5

Summary for 5C5X
Entry DOI10.2210/pdb5c5x/pdb
Related3D9S
DescriptorAquaporin-5, O-[(S)-{[(2S)-2-(hexanoyloxy)-3-(tetradecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-D-serine (3 entities in total)
Functional Keywordstransport protein, membrane protein
Biological sourceHomo sapiens (Human)
Cellular locationApical cell membrane ; Multi-pass membrane protein : P55064
Total number of polymer chains8
Total formula weight207193.69
Authors
Kitchen, P.,Oeberg, F.,Sjoehamn, J.,Hedfalk, K.,Bill, R.M.,Conner, A.C.,Conner, M.T.,Toernroth-Horsefield, S. (deposition date: 2015-06-22, release date: 2015-12-02, Last modification date: 2024-01-10)
Primary citationKitchen, P.,Oberg, F.,Sjohamn, J.,Hedfalk, K.,Bill, R.M.,Conner, A.C.,Conner, M.T.,Tornroth-Horsefield, S.
Plasma Membrane Abundance of Human Aquaporin 5 Is Dynamically Regulated by Multiple Pathways.
Plos One, 10:e0143027-e0143027, 2015
Cited by
PubMed Abstract: 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 Sjögren'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.
PubMed: 26569106
DOI: 10.1371/journal.pone.0143027
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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