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High-resolution x-ray structure of human aquaporin 5

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Author

Summary, in English

Human aquaporin 5 (HsAQP5)facilitates the transport of water across plasma membranes and has been identified within cells of the stomach, duodenum, pancreas, airways, lungs, salivary glands, sweat glands, eyes, lacrimal glands, and the inner ear. AQP5, like AQP2, is subject to posttranslational regulation by phosphorylation, at which point it is trafficked between intracellular storage compartments and the plasma membrane. Details concerning the molecular mechanism of membrane trafficking are unknown. Here we report the x-ray structure of HsAQP5 to 2.0-angstrom resolution and highlight structural similarities and differences relative to other eukaryotic aquaporins. A lipid occludes the putative central pore, preventing the passage of gas or ions through the center of the tetramer. Multiple consensus phosphorylation sites are observed in the structure and their potential regulatory role is discussed. We postulate that a change in the conformation of the C terminus may arise from the phosphorylation of AQP5 and thereby signal trafficking.

Publishing year

2008

Language

English

Pages

13327-13332

Publication/Series

Proceedings of the National Academy of Sciences

Volume

105

Issue

36

Document type

Journal article

Publisher

National Academy of Sciences

Topic

  • Biological Sciences

Keywords

  • heterologous overexpression
  • crystallography
  • water channel protein
  • trafficking
  • membrane protein

Status

Published

ISBN/ISSN/Other

  • ISSN: 1091-6490