Aquaporin-2 trafficking is regulated by PDZ-domain containing protein SPA-1
| Autor: | Michio Kuwahara, Yumi Noda, Tatsuo Kinashi, Keiji Hirai, Yoshifumi Katayama, Tomoki Asai, Koko Katagiri, Tetsushi Furukawa, Masakazu Hattori, Sei Sasaki, Nagahiro Minato, Saburo Horikawa |
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| Rok vydání: | 2004 |
| Předmět: |
Molecular Sequence Data
PDZ domain Mutant Biophysics Fluorescent Antibody Technique Biology Aquaporins urologic and male genital diseases Biochemistry Cell Line Dogs Structural Biology Genetics Animals PDZ protein Molecular Biology Trafficking Aquaporin 2 urogenital system rap1 GTP-Binding Proteins Colocalization Cell Biology Apical membrane Rats Cell biology Protein Transport Aquaporin 3 Rap1 Signal transduction Aquaporin-2 Signal Transduction |
| Zdroj: | FEBS Letters. 568:139-145 |
| ISSN: | 0014-5793 |
| Popis: | Targeted positioning of water channel aquaporin-2 (AQP2) strictly regulates body water homeostasis. Trafficking of AQP2 to the apical membrane is critical to the reabsorption of water in renal collecting ducts. Controlled apical positioning of AQP2 suggests the existence of proteins that interact with AQP2. A biochemical search for AQP2-interacting proteins led to the identification of PDZ-domain containing protein, signal-induced proliferation-associated gene-1 (SPA-1) which is a GTPase-activating protein (GAP) for Rap1. The distribution of SPA-1 coincided with that of AQP2 in renal collecting ducts. The site of colocalization was concomitantly relocated by hydration status. AQP2 trafficking to the apical membrane was inhibited by the SPA-1 mutant lacking Rap1GAP activity and by the constitutively active mutant of Rap1. AQP2 trafficking was impaired in SPA-1-deficient mice. Our results show that SPA-1 directly binds to AQP2 and regulates at least in part AQP2 trafficking. |
| Databáze: | OpenAIRE |
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