Water channel activities of  Mimosa pudica  plasma membrane intrinsic proteins are regulated by direct interaction and phosphorylation | Zendy

Temmei Yusuke | Zendy; Uchida Shinichi | Zendy; Hoshino Daisuke | Zendy; Kanzawa Nobuyuki | Zendy; Kuwahara Michio | Zendy; Sasaki Sei | Zendy; Tsuchiya Takahide | Zendy

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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 , protein phosphorylation , immunoprecipitation , biochemistry , microbiology and biotechnology , biology , mutagenesis , chemistry , biophysics , protein kinase a , botany , mutation , 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.

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