Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052690 | FEBS Letters | 2005 | 5 Pages |
Abstract
A direct interaction of the regulatory domain (R domain) of the cystic fibrosis transmembrane conductance regulator protein (CFTR) with PR65, a regulatory subunit of the protein phosphatase 2A (PP2A), was shown in yeast two hybrid, pull-down and co-immunoprecipitation experiments. The R domain could be dephosphorylated by PP2A in vitro. Overexpression of the interacting domain of PR65 in Caco-2 cells, as well as treatment with okadaic acid, showed a prolonged deactivation of the chloride channel. Taken together our results show a direct and functional interaction between CFTR and PP2A.
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Authors
Annick Vastiau, Lishuang Cao, Martine Jaspers, Grzegorz Owsianik, Veerle Janssens, Harry Cuppens, Jozef Goris, Bernd Nilius, Jean-Jacques Cassiman,