Membrane trafficking of AQP5 and cAMP dependent phosphorylation in bronchial epithelium

Janghee Woo, Young Kwang Chae, Se Jin Jang, Myoung Sook Kim, Jin Hyen Baek, Jong Chul Park, Barry Trink, Edward Ratovitski, Taekyul Lee, Beomsoo Park, Minjoo Park, Ji Hye Kang, Jean Charles Soria, Juna Lee, Joseph Califano, David Sidransky, Chulso Moon*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

46 Scopus citations


Phosphorylation pathway has been identified as an important step in membrane trafficking for AQP5. We generated stably transfected BEAS-2B human bronchial epithelial cells with various over-expression constructs on permeable support. In stable cells with wild-type AQP5 and S156A (AQP5 mutant targeting PKA consensus sequence), AQP5 expression was predominantly polarized to the apical membrane, whereas stable cells with N185D (AQP5 mutant targeting second NPA motif), mainly localized to the cytoplasm. Treatment with H89 and/or chlorophenylthio-cAMP (cpt-cAMP) did not affect membrane expression of AQP5 in any of three stable cells. In cells with wild-type AQP5 and N185D, AQP5s were phosphorylated by PKA, while phosphorylation of AQP5 was not detected in cells with S156A. These results indicate that, in AQP5, serine156 may be phosphorylated by PKA, but membrane expression of AQP5 may not be regulated by PKA phosphorylation. We conclude that AQP5 membrane targeting can include more than one mechanism besides cAMP dependent phosphorylation.

Original languageEnglish (US)
Pages (from-to)321-327
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Feb 8 2008


  • AQP5
  • Aquaporin
  • Membrane localization
  • cAMP dependent phosphorylation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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