High-resolution x-ray structure of human aquaporin 5
Artikel i vetenskaplig tidskrift, 2008

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-Å 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.

Författare

Rob Horsefield

Göteborgs universitet

Kristina Norden

Lunds universitet

Maria Fellert

Lunds universitet

Anna Backmark

Chalmers, Kemi- och bioteknik

Susanna Törnroth-Horsefield

Göteborgs universitet

Anke C. Terwisscha van Scheltinga

Max Planck-institutet

Jan Kvassman

Hogskolan i Kalmar

P. Kjellbom

Lunds universitet

Urban Johanson

Lunds universitet

Richard Neutze

Göteborgs universitet

Proceedings of the National Academy of Sciences of the United States of America

0027-8424 (ISSN) 1091-6490 (eISSN)

Vol. 105 36 13327-13332

Ämneskategorier

Kemi

DOI

10.1073/pnas.0801466105