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Water channel activities of Mimosa pudica plasma membrane intrinsic proteins are regulated by direct interaction and phosphorylation
Author(s) -
Temmei Yusuke,
Uchida Shinichi,
Hoshino Daisuke,
Kanzawa Nobuyuki,
Kuwahara Michio,
Sasaki Sei,
Tsuchiya Takahide
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.2005.06.082
Subject(s) - phosphorylation , mimosa pudica , aquaporin , biochemistry , protein phosphorylation , immunoprecipitation , chemistry , chaps , microbiology and biotechnology , biology , biophysics , membrane , protein kinase a , botany , gene
cDNAs encoding aquaporins PIP1;1, PIP2;1, and TIP1;1 were isolated from Mimosa pudica (Mp) cDNA library. MpPIP1;1 exhibited no water channel activity; however, it facilitated the water channel activity of MpPIP2;1 in a phosphorylation‐dependent manner. Mutagenesis analysis revealed that Ser‐131 of MpPIP1;1 was phosphorylated by PKA and that cooperative regulation of the water channel activity of MpPIP2;1 was regulated by phosphorylation of Ser‐131 of MpPIP1;1. Immunoprecipitation analysis revealed that MpPIP1;1 binds directly to MpPIP2;1 in a phosphorylation‐independent manner, suggesting that phosphorylation of Ser‐131 of MpPIP1;1 is involved in regulation of the structure of the channel complex with MpMIP2;1 and thereby affects water channel activity.