Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/34785
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Type: Journal article
Title: A fascinating tail: cGMP activation of aquaporin-1 ion channels
Author: Boassa, D.
Yool, A.
Citation: Trends in Pharmacological Sciences, 2002; 23(12):558-562
Publisher: Elsevier Science London
Issue Date: 2002
ISSN: 0165-6147
1873-3735
Statement of
Responsibility: 
Daniela Boassa and Andrea J. Yool
Abstract: Aquaporin-1 (AQP1) is a member of the diverse major intrinsic protein family of water and solute channels. AQP1 is known as an osmotic water channel in kidney, brain, vascular system and other tissues, and recently has been demonstrated to function as a cation channel gated by cGMP. Electrophysiology and binding assays implicate direct cGMP binding in the AQP1 C-terminus and sequence similarities with cyclic-nucleotide-gated channels support the idea that the AQP1 C-terminus mediates ion channel activation. In this article, new data show that the AQP1 C-terminus also exhibits homology, at key residues, with the substrate-selectivity subdomain of cyclic nucleotide phosphodiesterases. Distinct pathways for fluxes of water and ions in the tetrameric AQP1 channel indicate an intriguing multifunctional capacity. The physiological role of AQP1 in transmembrane signaling remains to be elucidated for these channels expressed in native tissues.
Keywords: Oocytes; Animals; Xenopus laevis; Humans; Aquaporins; Ion Channels; Cyclic GMP; Blood Group Antigens; Ion Channel Gating; Amino Acid Sequence; Sequence Homology, Amino Acid; Molecular Sequence Data; Aquaporin 1
Description: Copyright © 2002 Elsevier Science Ltd. All rights reserved.
RMID: 0020063451
DOI: 10.1016/S0165-6147(02)02112-0
Appears in Collections:Molecular and Biomedical Science publications

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