Noncanonical binding of calmodulin to aquaporin-0: implications for channel regulation.
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ABSTRACT:
SUBMITTER: Reichow SL
PROVIDER: S-EPMC2605016 | biostudies-literature | 2008 Sep
REPOSITORIES: biostudies-literature
Publications
Noncanonical binding of calmodulin to aquaporin-0: implications for channel regulation.
Reichow Steve L SL Gonen Tamir T
Structure (London, England : 1993) 20080901 9
Aquaporins (AQPs) are a family of ubiquitous membrane channels that conduct water across cell membranes. AQPs form homotetramers containing four functional and independent water pores. Aquaporin-0 (AQP0) is expressed in the eye lens, where its water permeability is regulated by calmodulin (CaM). Here we use a combination of biochemical methods and NMR spectroscopy to probe the interaction between AQP0 and CaM. We show that CaM binds the AQP0 C-terminal domain in a calcium-dependent manner. We de ...[more]
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