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Interaction of the protein phosphatase 2A with the regulatory domain of the cystic fibrosis transmembrane conductance regulator channel
Author(s) -
Vastiau Annick,
Cao Lishuang,
Jaspers Martine,
Owsianik Grzegorz,
Janssens Veerle,
Cuppens Harry,
Goris Jozef,
Nilius Bernd,
Cassiman Jean-Jacques
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.04.079
Subject(s) - cystic fibrosis transmembrane conductance regulator , regulator , phosphatase , conductance , chemistry , microbiology and biotechnology , cystic fibrosis , transmembrane protein , domain (mathematical analysis) , channel (broadcasting) , biophysics , biochemistry , biology , physics , computer science , genetics , phosphorylation , gene , receptor , mathematics , telecommunications , condensed matter physics , mathematical analysis
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.