Regulation of aquaporin-2 trafficking and its binding protein complex
書誌事項
- 公開日
- 2006-08
- 権利情報
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- https://www.elsevier.com/tdm/userlicense/1.0/
- https://www.elsevier.com/open-access/userlicense/1.0/
- DOI
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- 10.1016/j.bbamem.2006.03.004
- 公開者
- Elsevier BV
この論文をさがす
説明
Trafficking of water channel aquaporin-2 (AQP2) to the apical membrane is critical to water reabsorption in renal collecting ducts and its regulation maintains body water homeostasis. However, exact molecular mechanisms which recruit AQP2 are unknown. Recent studies highlighted a key role for spatial and temporal regulation of actin dynamics in AQP2 trafficking. We have recently identified AQP2-binding proteins which directly regulate this trafficking: SPA-1, a GTPase-activating protein (GAP) for Rap1, and cytoskeletal protein actin. In addition, a multiprotein "force generator" complex which directly binds to AQP2 has been discovered. This review summarizes recent advances related to the mechanism for AQP2 trafficking.
収録刊行物
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- Biochimica et Biophysica Acta (BBA) - Biomembranes
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Biochimica et Biophysica Acta (BBA) - Biomembranes 1758 (8), 1117-1125, 2006-08
Elsevier BV
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キーワード
- Biophysics
- Diabetes Insipidus, Nephrogenic
- Biochemistry
- Channel protein
- Rho
- Cyclic AMP
- Animals
- Humans
- Kidney Tubules, Collecting
- Phosphorylation
- Cytoskeleton
- Aquaporin 2
- Cell Membrane
- GTPase-Activating Proteins
- PKA phosphorylation
- Cell Polarity
- Cell Biology
- Actins
- Endocytosis
- Protein Structure, Tertiary
- Arginine Vasopressin
- Protein Transport
- Mutation
- Calcium
- Vasopressin
- Protein Binding
詳細情報 詳細情報について
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- CRID
- 1361699993533282176
-
- NII論文ID
- 30003024727
-
- ISSN
- 00052736
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- PubMed
- 16624255
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- データソース種別
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- Crossref
- CiNii Articles
- OpenAIRE
