5DYE

CRYSTAL STRUCTURE OF THE FULL LENGTH S156E MUTANT OF HUMAN AQUAPORIN 5

5DYE の概要

• エントリーDOI: 10.2210/pdb5dye/pdb
• 関連するPDBエントリー: 3D9S 5C5X
• 分子名称: Aquaporin-5, O-[(S)-{[(2S)-2-(hexanoyloxy)-3-(tetradecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-D-serine (2 entities in total)
• 機能のキーワード: transport protein, membrane protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Apical cell membrane ; Multi-pass membrane protein : P55064
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 113984.07

構造登録者

Kitchen, P.,Oeberg, F.,Sjoehamn, J.,Hedfalk, K.,Bill, R.M.,Conner, A.C.,Conner, M.T.,Toernroth-Horsefield, S. (登録日: 2015-09-24, 公開日: 2015-12-02, 最終更新日: 2024-05-08)

主引用文献

Kitchen, 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

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

実験手法

X-RAY DIFFRACTION (3.5 Å)