Regulation of Plasma Membrane Nanodomains of the Water Channel Aquaporin-3 Revealed by Fixed and Live Photoactivated Localization Microscopy

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  • Eva C. Arnspang
  • Prabuddha Sengupta, National Institutes of Health, Janelia Research Campus
  • ,
  • Kim I. Mortensen, Danmarks Tekniske Universitet
  • ,
  • Helene H. Jensen
  • ,
  • Ute Hahn
  • Eva B.V. Jensen
  • Jennifer Lippincott-Schwartz, National Institutes of Health, Janelia Research Campus
  • ,
  • Lene N. Nejsum

Several aquaporin (AQP) water channels are short-term regulated by the messenger cyclic adenosine monophosphate (cAMP), including AQP3. Bulk measurements show that cAMP can change diffusive properties of AQP3; however, it remains unknown how elevated cAMP affects AQP3 organization at the nanoscale. Here we analyzed AQP3 nano-organization following cAMP stimulation using photoactivated localization microscopy (PALM) of fixed cells combined with pair correlation analysis. Moreover, in live cells, we combined PALM acquisitions of single fluorophores with single-particle tracking (spt-PALM). These analyses revealed that AQP3 tends to cluster and that the diffusive mobility is confined to nanodomains with radii of ∼150 nm. This domain size increases by ∼30% upon elevation of cAMP, which, however, is not accompanied by a significant increase in the confined diffusion coefficient. This regulation of AQP3 organization at the nanoscale may be important for understanding the mechanisms of water AQP3-mediated water transport across plasma membranes.

TidsskriftNano Letters
Sider (fra-til)699-707
Antal sider9
StatusUdgivet - feb. 2019

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