Water channel activities of <i>Mimosa pudica</i> plasma membrane intrinsic proteins are regulated by direct interaction and phosphorylation

• Yusuke Temmei

• Shinichi Uchida

• Daisuke Hoshino

• Nobuyuki Kanzawa

• Michio Kuwahara

• Sei Sasaki

• Takahide Tsuchiya

抄録

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.

収録刊行物

• FEBS Letters

  FEBS Letters 579 (20), 4417-4422, 2005-07-20

  Wiley

キーワード

• Cell Biology
• Genetics
• Molecular Biology
• Biochemistry
• Structural Biology
• Biophysics

詳細情報

• CRID: 1361137044532863488
• NII論文ID: 80017410199
• DOI: 10.1016/j.febslet.2005.06.082
• ISSN: 18733468
• ISSN: 00145793
• Web Site: https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2Fj.febslet.2005.06.082
• Web Site: https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/j.febslet.2005.06.082
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