Water channel activities of Mimosa pudica plasma membrane intrinsic proteins are regulated by direct interaction and phosphorylation
Copyright policy )Water channel activities of Mimosa pudica plasma membrane intrinsic proteins are regulated by direct interaction and phosphorylation
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.
- Institute of Science Tokyo Japan
- Sophia University Japan
Mimosa pudica, Mimosa, Aquaporin, Xenopus, Cell Membrane, Plasma membrane intrinsic protein, Membrane Proteins, Aquaporins, Cyclic AMP-Dependent Protein Kinases, cAMP-dependent protein kinase A, Direct interaction, Mutagenesis, Oocytes, Animals, Immunoprecipitation, Phosphorylation, Gene Library, Plant Proteins
Mimosa pudica, Mimosa, Aquaporin, Xenopus, Cell Membrane, Plasma membrane intrinsic protein, Membrane Proteins, Aquaporins, Cyclic AMP-Dependent Protein Kinases, cAMP-dependent protein kinase A, Direct interaction, Mutagenesis, Oocytes, Animals, Immunoprecipitation, Phosphorylation, Gene Library, Plant Proteins
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