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Single amino acids in the carboxyl terminal domain of aquaporin-1 contribute to cGMP-dependent ion channel activation
Authors:Daniela?Boassa,Andrea?J?Yool  author-information"  >  author-information__contact u-icon-before"  >  mailto:ayool@u.arizona.edu"   title="  ayool@u.arizona.edu"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author
Affiliation:(1) Program in Neuroscience, University of Arizona, Tucson, Arizona 85724-5051, USA;(2) Dept. of Physiology, University of Arizona College of Medicine, Tucson, Arizona, USA;(3) Dept. of Pharmacology, University of Arizona College of Medicine, Tucson, Arizona, USA
Abstract:

Background  

Aquaporin-1 (AQP1) functions as an osmotic water channel and a gated cation channel. Activation of the AQP1 ion conductance by intracellular cGMP was hypothesized to involve the carboxyl (C-) terminus, based on amino acid sequence alignments with cyclic-nucleotide-gated channels and cGMP-selective phosphodiesterases.
Keywords:
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